Food engineering has been on an incredibly strange journey, but there is none stranger (at least to me) than the concept of in vitro meat. Colloquially referred to as “shmeat,” a term born out of mashing up the phrase “sheets of meat,” in vitro meat may be available in our grocer’s refrigerator section in just a few years. But how exactly is shmeat produced and how does it compare to, you know, that which is derived from actual animals? Here, I hope to shed some light on this petri dish to kitchen dish phenomenon.
The shmeaty deets
When it comes to producing shmeat, scientists are taking advantage the extensive cell culture technologies that have been developed over the course of the 20th century (for a brief history of these developments, check this out). Because of what we have learned, we can easily determine the conditions under which cells grow best, and swiftly turn a few cells into a few million cells. However, things can get a little tricky when growing complex, three-dimensional tissues like steak or boneless chicken breast.
For instance, lets consider a living, breathing cow. Most people seem to enjoy fancy cuts like beef tenderloin, which, before the butcher gets to it, is located near the back of the cow. In order for that meat to be nice and juicy, it needs to have enough nutrients and oxygen to grow. In addition, muscles (in this case, the tenderloin) need stimulation, and in the cow (and us too!) that is achieved by flexing and relaxing.
If shmeat is to be successfully engineered, scientists need to replicate all of the complexities that occur during the normal life of an actual animal. While the technology for making shmeat is still being optimized, the components involved in this meat-making scheme successfully address many of the major issues with growing whole tissues in a laboratory.
The first step in culturing meat is to get some muscle cells from an animal. Because cells divide as they grow, a single animal could, in theory, provide enough cells to make meat for many, many people – and for a long period of time. However, the major hurdle is creating a three-dimensional tissue, you know, something that would actually resemble a steak.
Normally, cells will grow in a single layer on a petri dish, with a thickness that can only be measured by using a microscope. Obviously that serving size would not be very satisfying. In order to create that delicious three-dimensional look, feel, and taste, and be substantial enough to count as a meal, scientists have developed a way to grow the muscle cells on scaffold made of natural and edible material. As sheets of cells grow on these scaffolds, they are laid on top of each other to bulk up the shmeat (hence “sheets of meat”). But, in order for the cells on the inside of this 3D mass to grow as well as the cells on the outside, there has to be an sufficient way to deliver nutrients and oxygen to all cells.
Back to the tenderloin – when it is still in the cow, the cells that make up this piece of meat are in close contact to a series of veins, arteries, and capillaries. Termed vasculature, this system allows for the cells to obtain nutrients and oxygen, while simultaneously allowing cells to dump any waste into the blood stream. There are some suggestionsthat the shmeat can be vascularized (grown such that a network of blood vessels are formed); however, the nutrient delivery system most widely used at this point is something called a bioreactor.
This contraption is designed to support biologically active materials and how it works is actually quite cool. The cells are placed in the cylindrical bioreactor, which spins at a rate that balances multiple physical forces, which keep the entire cell mass fully submerged in liquid growth medium at all times. This growth medium is constantly refreshed, ensuring that the cells are always supplied with a maximum level of growth factors. In essence, the shmeat is kept in a perpetual free fall state while it grows.
But there is one last piece to the meat-growing puzzle, and that is regular exercise. If we look at meat on a purely biological level, we would see that it is just a series of cells arranged to form muscle tissue. Without regular stimulation, muscles will waste away (atrophy). Clearly, wasting shmeat would not be very efficient (or tasty). So, shmeat engineers have reduced the basic biological process involved with muscle stimulationto the most basic components – mechanical contraction and electrical stimulation. Though mechanical contraction (the controlled stretching and relaxing of the growing muscle fibers) has been shown to be effective, it is not exactly feasible on a large scale. Electrical stimulation – the process of administering regular electrical pulses to the cells – is actually more effective than mechanical contraction and can be widely performed. Therefore, it seems to be a more viable option for shmeat production.
Why in the world would we grow meat in a petri dish?
Grill it, braise it, broil it, roast it – as long as it tastes good, most people don’t usually question the origins of their meat. Doing so could easily make one think twice about what they are eating. Traditionally speaking, every slab of meat begins with a live animal – cow, pig, lamb, poultry (yes, despite what my grandmother says, this vegetarian does consider chicken to be meat) – with each animal only being able to provide a finite number of servings. While shmeat does ultimately begin with a live animal, only a few muscle, fat, and other cells are required.
Given the theoretical amount that can be produced with just a few cells, the efficiency of traditional meat-generating farms and slaughterhouses is becoming increasingly scrutinized. There are obvious costs – economic, agricultural, environmental – that are associated with livestock, and it has been proposed(article behind dumb pay wall, grrrr….) that shmeat engineering would substantially cut these costs. For instance, it has been projected that shmeat production could use up to 45% less energy, compared to traditional farming methods. Furthermore, relative to the current meat production process, culturing shmeat would use 99% less land, 82-96% less water, and would significantly reduce the amount of greenhouse gasesproduced.
The impact of shmeat compared to tradtional agricultural processes. (Environ. Sci. Technol., 2011, 45 (14), pp 6117–6123)
But the potential benefits of making the shift toward shmeat (as opposed to meat) doesn’t stop with its positive environmental impact. From a nutritional standpoint, it is possible to produce shmeat in a way that would significantly reduce the amount of saturated fat it contains. Additionally, there are technologies that would allow shmeat to be enriched with heart-healthy omega-3 fats, as well as other types of polyunsaturated fats. In essence, shmeat could possibly help combat our growing obesity epidemic, as well as the associated illnesses such as diabetes and heart disease. That’s *if* it can be produced in a way that is both affordable and widely available (more on that in a bit).
In terms of health, switching to shmeat would improve more than our waistlines. Because shmeat would be produced in a sterile environment, the incidence of E. coli and other bacterial and/or viral contamination would be next to nothing relative to current meat production methods. On a more superficial level, shmeat technology would allow for the introduction of some very exotic meats into the mainstream. Because this technology does not require an animal to be slaughtered (another good reason that supports shmeat productions) and it is not limited to the more common sources of meat, it would be entirely possible to make things like panda sausage and crocodile burgers. But, of course, getting people to actually eat meat grown in a test-tube is another issue…
The limitations of shmeat
Now that I’ve just spent a few paragraphs singing shmeat’s praises, it is probably best that I fill you in on some of the major roadblocks associated with shmeat production. According to scientists, there are two main concerns: the first is that shmeat production will not be subjected to the normal regulatory (homeostatic) mechanisms that naturally occur in animals (scientists are having trouble figuring out how to replicate these processes); and the second is that shmeat engineering technology has not evolved enough so that it can occur on an industrial scale. Because of these issues and others, the cost of culturing shmeat in the laboratory is very high. But, there has always got to be a starting point. As the technologies advance, the cost-production ratios will decrease and, eventually, shmeat will find its way to the dining table – our dining table.
Interestingly, the folks at PETA are all for shmeat and offered a one million dollar prize to the first group who could come up with the technology to make shmeat commercially available by June, 2012. Obviously, that did not happen, and the contest has been extended to January 2013 (this offer has been on the table since 2008). But, the first tastes test for shmeat hamburgers is going down in October of this year.
At the moment, the largest piece of shmeat to be created is about the size of a contact lens and my guess is that, barring unforeseen technological breakthroughs, this reward will go unclaimed for a long, long time. But, many a miracle has been known to happen in about nine months time…
A few final thoughts on shmeat
With the world population expected to hit 9 billion by 2050, which will be accompanied by a major increase in the need for the amount of food produced, perhaps shmeat technology will become one of the critical innovations required for our collective survival on this planet. But, there is just one thing: the ick factor. It is a little hard for me to weigh in on this issue because almost all meat seems gross to me (unless it is a pulled pork sandwich, lovingly made by my long-time pal and professional chef – Julie Hall). While most of my peers have less of an aversion to meat, I can’t imagine that they would eagerly line up for a whopping serving of lab-grown shmeat.
But, say scientists finally figure it out and shmeat production is scaled up for mass consumption – how will the agricultural sector react? As of right now, the agricultural industry in the USA is worth over $70 billion, with a yearly beef consumptiontipping over the 26 million pound mark (of which 8.7% is exported). Shmeat probably has definitely gotten the attention of cattle farmers (and other meat farmers/production companies) and, given the size of this industry, I wonder how much muscle will be used to block shmeat from becoming a household phenomenon.
Over all, I think that shmeat is a revolutionary idea as it could have a significant impact on humanity. However, there are many complex questions that need to be both asked andanswered. As excited as I am at the thought of not having to kill an animal to eat a steak, I still remain skeptical (though this sentiment may not have been fully present for the majority of this post). Will shmeat be produced in such a way that it will be indistinguishable from traditional meat? Additionally, will shmeat live up to all of these expectations? I am going to try and keep a positive outlook with this one. Perhaps the next time I actually step foot in a kitchen to prepare a meal, I’ll follow Randy’s lead by making a shmeatloaf, served alongside a heaping side of mashed potatoes. Now that’s some pretty cool kitchen science.
And now, an oldie but a goodie (let it be known that I am in love with Stephen Colbert):
If a child is diagnosed with autism spectrum disorder (ASD), it is because they have gone through a number of rigorous behavioral tests, often over a period of time, and never straightforward. Of course, this time can be a stressful for parents or caregivers, and sometimes the answers can lead to even more questions. One solution to the waiting and uncertainty would be to have a medical test that could more easily diagnose ASD. However, no one has been able to identify biomarkers – molecules in the body that can help define a specific medical condition – for the condition. Without this type of information, it is not possible to create a diagnostic test for autism.
Having been through this process with their son, who is on the autism spectrum, Clarkson University scientists Costel Darie and Alisa Woods have decided to work together to help address this issue. An interdisciplinary laboratory that combines hardcore proteomics (the study of the proteins we make) with cognitive neuroscience is probably not what you think of when it comes to running a family business. But for Darie and Woods, “marriage” has many meanings. This husband and wife team has combined their brainpower to embark on a scientific journey toward understanding some of the biochemistry behind autism, and they are walking on an increasingly popular path to help finance their work: crowdfunding.
A major goal of the Darie Lab is to identify biomarkers that are associated with autism and then to create a medical test to help alleviate some of the frustrations that come with the ASD diagnostic process. Using a technology called high-definition mass spectrometry, the Darie Lab has outlined a project to figure out the types of proteins that are in the saliva or blood of children with ASD and compare these protein profiles to the saliva or blood from children who are not on the autism spectrum. If the Darie Lab is successful, they might be able to help create a diagnostic test for early autism detection, which would undoubtedly fill a giant void in the field of autism research and treatment.
Here is how the experiment will work: The members of the Darie Lab will collect saliva (and/or blood) samples from children, half of whom are on the autism spectrum and half of whom are not. The researchers will prepare the saliva or blood and collect the proteins. Each protein will be analyzed by a high definition mass spectrometer, which is basically a small scale for measuring the weight and charge of a protein. The high definition mass spectrometer will transfer information about the proteins to a computer, with special software allowing the Darie Lab investigators to figure out the exact makeup of proteins in each sample.
The bottleneck when it comes to these experiments is not getting samples (saliva and blood are easy to collect), and it isn’t the high-tech high-definition mass spectrometer because they have access to one. Rather, the bottleneck comes from the very high cost of the analytical software they need. Because this software was not included in their annual laboratory budget but is critical to conducting this experiment, the Darie Lab is raising money through crowdfunding.
Why I think a contribution is worth the investment: Technology is always advancing, especially when it comes to protein biochemistry. The high-definition mass spectrometer is a recent technology, and according to the Darie Lab, they have been able to identify over 700 proteins in the saliva alone. This is quite an incredible step up from traditional mass spectrometers, which could detect only around 100 proteins in saliva. Just because we haven’t been able to identify biomarkers for autism in the past doesn’t mean we can’t do it now.
In addition to the use of this new technology, the Darie Lab presents some compelling preliminary evidence for a difference in protein profiles between those with ASD and those who do not have ASD. While they’ve examined only three autistic people and compared them to three non-ASD individuals, the two groups were clearly distinct in their saliva protein profiles. If this pattern holds up with an increased number of study participants, the implications could be quite significant for autism research.
Preliminary data from the Darie Lab shows that there are saliva proteins showing a 20X or greater difference between ASD (ovals) versus sibling non-ASD controls (rectangles).
If you decide to kick in some funds, your good deed will not go unrewarded. As a thank-you for contributing, the Darie Lab has offered up a few cool perks, including high-quality prints of microscopic images in the brain.
If you are looking for a good cause, look no further. I am excited to see how the Darie Lab crowdfund experience goes, and I wish them all the best in their quest, both as professionals and as parents. To find out more, or to make a donation, visit the Darie Lab RocketHub page.
Fluorescent images of the brain, available to those donating $100 or more.
The opinions expressed in this post do not necessarily agree or conflict with those of the DXS editorial team and contributors.
Leah Gerber is an Associate Professor of ecology at Arizona State University. Her research is motivated by a desire to connect academic pursuits in conservation science to decision tools and effective conservation solutions. This approach includes a solid grounding in natural history and primary data collection, quantitative methods and an appreciation for the interactions between humans and the environment. She is keenly aware of the need for the communication of scientific results to the public and to government and non-governmental agencies. This communication is essential for the translation of scientific results into tenable conservation solutions.
DXS: First, can you give me a quick overview of what your scientific background is and your current connection to science?
LG: I learned about ecology and environmental conservation as an undergraduate and quickly became motivated to do science that impacted the real world of conservation. Learning about the impacts of humans on nature was a wake-up call for me, and inspired me to channel my feeling of concern for the demise of nature in a positive way.
From there, I have walked the tightrope between science and policy. After getting my undergraduate degree in environmental biology, I wanted to do more than just the science. So I enrolled in a masters program at the University of Washington – an interdisciplinary program called Marine Affairs. It was a great experience, but I wanted to have more substance to my science background – I wanted to know how to do the science in addition to how to apply the science.
This compelled me to enter a PhD at the University of Washington, which was largely funded by NOAA. My thesis involved trying to figure out how to make decisions about endangered species – how to determine which were endangered and which were threatened. This was a perfect project given my interest in developing tools to solve problems. After finishing my PhD, I did a postdoc at the National Center for Ecological Analysis and Synthesis (NCEAS) and developed approaches for marine reserve design and endangered species recovery. I was at NCEAS for three years before starting on the tenure track at Arizona State University. I’ve been at ASU for about 10 years now.
A major theme in my work has remained constant – that is, how to use the information we are generating in the natural and social sciences to better manage our natural world. Pre-tenure I focused a lot more on doing the science, publishing in good journals, and hoping that it made its way into good policy. Now that I am midcareer, meaning that I have a good amount of papers and tenure, I am enjoying the opportunity to work with practitioners outside of academia. For instance, I just got off the phone with someone from National Geographic regarding my recent publicationon seafood health and sustainability. In that study, we performed an analysis regarding seafood in the context of health and sustainability, to answer simple questions like, what to order when out to sushi? How do we educate about health benefits and risks? We will be organizing a workshop to help restaurant chains, grocery stores, as well as environmental NGOs identify a path forward in informing consumers about healthy and sustainable seafood choices. As a tenured professor, I feel fortunate to have the opportunity to work at the science-policy interface and to give society some science that is truly applicable.
DXS: It is too bad that you have to wait until you are more established and have tenure to go out and engage with the public, because this type of thing is just so important!
LG: Yes, I agree. There isn’t a clear path in academia when it comes to public engagement. But in recent years I have felt optimistic – the landscape within academia is starting to change, and at ASU this change is noticeable. We have a fabulous president, Michael Crow, who has really transformed ASU from just another state institution to a leader in sustainability. Part of this is the establishment of the Global Institute for Sustainability, and one of Michael Crow’s mantras is “community embeddedness.” He is really on board with this type of thing and I have seen evidence of his commitment trickle down throughout the University. For instance, when I first arrived, I had to justify and explain why I was serving on these federal recovery teams for endangered species. Now I feel that there is no justification needed. Developing solutions is not only so important for society, but should also be a key aspect of what we do at Universities.
DXS: We were introduced by another fantastic science communicator, Liz Neeley, who you met at a communications workshop. Why is it important to take part in this type of training?
LG: I met the Fantastic and Fashionable Liz through the Leopold Leadership Program, offered through the Woods Institute for the Environment at Stanford University. The Leopold Leadership training was the best professional development experience of my career, and has made me a better translator and communicator of science to policy. Pre-Leopold, I had little training in communications, and there I was, in a teaching position where I taught hundreds students. I thought to myself, well, how do I do this? The Leopold experience has solidified my commitment to teaching students about communication and engaging in policy.
One development emerging from this training is a science communication symposium at the AAAS meeting. Elena Bennett and I are giving a talk on overcoming institutional barriers for community engagement, and we will address the issues head on. We put out a survey asking others if they faced institutional barriers, and how they might work to engage more.
DXS: What ways do you express yourself creatively that may not have a single thing to do with science?
LG: I have 2 young kids, a 3yo and a 7yo. Being a mom helps me keep it real - I love that I get to enjoy the awe of discovering the world with my girls. We just got a puppy this weekend and we are having fun dressing her up and painting her nails (only partly joking). Other things that I do that are creative – truthfully, I am uninteresting – I don’t bake bread or go to the opera. I just work and take care of my kids. I practice yoga for my own sanity and also love to work in the garden. Doing these things gives me a reason to pause and step off the treadmill of keeping up with everything.
DXS: Do you find that your scientific background informs the creativity you have with your kids or your yoga practice, even though what you do may not specifically be scientific?
LG: I think there is synergy with my science and my kids and my yoga practice in helping me to accept things and be mindful – but not in any conscious way. For instance, when doing my science, the type A person that I am, I have an inclination to keep pushing, pushing, pushing. My kids and my yoga help me to shift gears and accept that things are going to happen when they happen. I try to let the kids be kids, including the associated chaos, and accept that this is a snapshot in time that they will be little. Now I find joy in that chaos. Having kids and yoga gives me a little more perspective, and the knowledge that things aren’t lined up and neatly placed in a box. It rounds me out.
DXS: Are your kids are major influencers in your career?
LG: My first child, Gabriella, was born just after I submitted my application for tenure – so it was good timing. And I was able to slow down. I quickly realized that I wasn’t able to work a 60+hour week. Before kids, I lived to work. Now, I work to live. I absolutely love my job and I feel so lucky that I have a career that I believe in and that I am actually paid to do it – it’s not just a hobby. But having kids made me chill out a little. If I get a paper rejected, I can let it go instead of lamenting about it for weeks. It has made me healthier. I don’t necessarily know if it has had positive impact on my career – time will tell. While my publication rate may be slightly smaller, I think my work now has different dimensions, and greater depth.
I am still pretty passionate about my work, and my kids know what I do and are proud of it. They share it with their classmates, and take every opportunity to wax poetic about how their mom saves animals in the ocean. They also have a built in conservation effort – my 7YO gets irritated when she can’t find a compost bin, and her new thing is to only fill her cup half way because she will only drink a little bit of water.
DXS: When you decided to have children, did your colleagues view you differently? Did they consider that you were sending your career down the tubes or was it a supportive environment?
LG: I honestly had a really positive experience. I can’t think of any negative sentiments from my colleagues, and they were actually really supportive. For instance, when I was pregnant with my first daughter, ASU did not have a maternity leave policy. Before that, you would have to take sick leave. So my colleague worked within the parameters of the unit to give me maternity leave. And then with my second daughter, our new president had established a maternity policy.
The support of my colleagues at ASU has made me feel loyal to my institution. Normally, I am loyal to people and not institutions, but overall, the support has been fabulous. Of course, with having the kids in each case, I did decline a lot of invitations – some pretty significant ones – but I did not have a desire to drag a newborn to give a talk, especially when I was nursing. And it was hard for me to do this at times, especially given my career driven nature, and I had to learn to accept that there would be other opportunities.
I had to shift it down a notch and realize that the world wasn’t going to freeze over, and that I could shift it back to high gear later. With “mommy brain”, I knew I wasn’t going to be at the top of my game at that point in my life. But I have incredible role models. Most notable is Jane Lubchenco, currently the Director of the National Oceanic and Atmospheric Administration. During the first part of her career, she shared a position with her husband – each did 50% – and they did that on purpose so they’d be able to enjoy having children and effectively take care of them. Now, she is in the National Academy, is having major scientific impacts, and she did it all despite having kids. If she can do it, why cant the rest of us?
DXS: Given your experiences as a researcher, as a mother, and now as a major science communicator, do you feel that your ability to talk to people has evolved?
LG: Absolutely. I think that the Leopold Training Program, which selects 20 academics from North America to participate in retreats to learn how to be better communicate and lead, has re-inspired all who attended. It has recharged our batteries and allowed us to make realizations that doing good science and putting it out there via scientific publication is just not enough. We also have to push it out there and make it available to a broader, more diverse population. As part of the training, we also learned about different thinking styles – super analytical or super emotional – and after I returned, I had my lab group participate in this type of exercise. And now I feel like I can better assess a persons thinking style and adjust the way I communicate accordingly.
DXS: Did you always have the ability to talk to the general public or does having kids help you to better understand some of the nuances associated with science communication?
LG: I think so. In fact, I am thinking back to when I had a paper in Sciencecome out around the time that I had my first child. It got a lot of news coverage and was featured in Time magazine. I thought it was so cool at the time, but looking back on it I realized that have come a long way. I said something to a journalist, who then asked me to translate it into “plain English.” It was a little bit of a jab.
Now, with kids, I can tell you a lot more about my research and can better see the broader impact. Talking to them helps me to do that. Here is a conversation about my research with my daughter:
L: Mama is working on figuring out how to help the whales that people like to eat. It’s a big problem because some people like to eat whales and some like to see them swimming in the ocean.
G: What we have to do is let the people eat the whales in the ocean, and buy some whales from the pet store to put back in the ocean. How much do whales cost?
L: Good idea. But you can’t buy whales at the store. They are too big. And if we take them all out of the ocean there will be none left.
G: Well instead we should ask the people to eat bad things like sharks.
L: Another good idea. But if we take sharks out there will be no predators to eat the big fish. And the whole ecosystem would collapse.=
G: Well then the people should eat other things like fish instead of whales. They should buy a fishing pole and catch a fish and eat those instead of whales.
L: What about chicken, shouldn’t people just eat chicken?
G: Mama, we can’t kill chickens. Chickens are nicer than fish, so that’s why we have to eat fish.
L: What about just eating vegetables?
G: Oh mama, some people are meat-eaters. And there are no more dinosaurs. They all got extinct. They should have saved some of the dinosaur meat in the freezer for the meat-eaters. When the dinosaurs come back, there will be enough meat to eat and people won’t want to eat whales.
The simplicity of taking myself out of my research bubble and engaging with a creative (and nonlinear?) 7YO has taught me how to be a better communicator – with the media, with my students, and with the general population.
DXS: Do you think these efforts in science communication are helping to shift other peoples perspectives about who a scientist actually is? For instance, are we changing the old crazy haired white guy stereotype?
LG: Well, I hope so. A couple of examples – again, as a mom, one of my daughters a Girl Scout and I get to help with the troop. One of the themes was to teach about environmental and conservations awareness. We did this Crayola molding experiment where we put our fingers into cold water. We then did the same thing except we put modeling clay over our fingers before putting them into the cold water and to learn about adaptations to extreme environments. Also, we play games where they simulate fishing – what if there is plastic? What happens to you if you eat that? My hope is that this shows these young girls that science is both interesting and fun.
Another thing that just happened today is that I was contacted by Martha Stewart’s office, and it seems that some of my research results will be featured in the October issue of Martha Stewart Living. The message here is that I happen to care about the ocean, but I also love sushi. I also I care about health. I am not just a nerd in a lab coat. I am a mom, I do yoga, I have wonderful friends, and here is the kind of science that I do. It seems to me that it is better to connect with others when I can give them something that is relevant to their lives instead of a more abstract ecological theory.
DXS: If you had something you could say to the younger you about getting on your chosen career path, what would you say?
LG: I feel like I have been very effective at figuring out how to get from point A to point B, but less successful at savoring the process. I think that I’d tell myself to make time to celebrate the small victories. I have also learned to identify what kind of research is most exciting, and I would tell myself to say “no” to everything that is only moderately interesting. I tell my grad students that if you don’t dive in head first, you won’t ever know. So why just not give it a try! And if it doesn’t work, move on. Also, if something isn’t making you happy, change! Academia isn’t for everyone, and there is a lot more to life than science.
The four basic categories of molecules for building life are carbohydrates, lipids, proteins, and nucleic acids.
Carbohydrates serve many purposes, from energy to structure to chemical communication, as monomers or polymers.
Lipids, which are hydrophobic, also have different purposes, including energy storage, structure, and signaling.
Proteins, made of amino acids in up to four structural levels, are involved in just about every process of life.
The nucleic acids DNA and RNA consist of four nucleotide building blocks, and each has different purposes.
The longer version
Life is so diverse and unwieldy, it may surprise you to learn that we can break it down into four basic categories of molecules. Possibly even more implausible is the fact that two of these categories of large molecules themselves break down into a surprisingly small number of building blocks. The proteins that make up all of the living things on this planet and ensure their appropriate structure and smooth function consist of only 20 different kinds of building blocks. Nucleic acids, specifically DNA, are even more basic: only four different kinds of molecules provide the materials to build the countless different genetic codes that translate into all the different walking, swimming, crawling, oozing, and/or photosynthesizing organisms that populate the third rock from the Sun.
Big Molecules with Small Building Blocks
The functional groups, assembled into building blocks on backbones of carbon atoms, can be bonded together to yield large molecules that we classify into four basic categories. These molecules, in many different permutations, are the basis for the diversity that we see among living things. They can consist of thousands of atoms, but only a handful of different kinds of atoms form them. It’s like building apartment buildings using a small selection of different materials: bricks, mortar, iron, glass, and wood. Arranged in different ways, these few materials can yield a huge variety of structures.
We encountered functional groups and the SPHONC in Chapter 3. These components form the four categories of molecules of life. These Big Four biological molecules are carbohydrates, lipids, proteins, and nucleic acids. They can have many roles, from giving an organism structure to being involved in one of the millions of processes of living. Let’s meet each category individually and discover the basic roles of each in the structure and function of life.
You have met carbohydrates before, whether you know it or not. We refer to them casually as “sugars,” molecules made of carbon, hydrogen, and oxygen. A sugar molecule has a carbon backbone, usually five or six carbons in the ones we’ll discuss here, but it can be as few as three. Sugar molecules can link together in pairs or in chains or branching “trees,” either for structure or energy storage.
When you look on a nutrition label, you’ll see reference to “sugars.” That term includes carbohydrates that provide energy, which we get from breaking the chemical bonds in a sugar called glucose. The “sugars” on a nutrition label also include those that give structure to a plant, which we call fiber. Both are important nutrients for people.
Sugars serve many purposes. They give crunch to the cell walls of a plant or the exoskeleton of a beetle and chemical energy to the marathon runner. When attached to other molecules, like proteins or fats, they aid in communication between cells. But before we get any further into their uses, let’s talk structure.
The sugars we encounter most in basic biology have their five or six carbons linked together in a ring. There’s no need to dive deep into organic chemistry, but there are a couple of essential things to know to interpret the standard representations of these molecules.
Check out the sugars depicted in the figure. The top-left molecule, glucose, has six carbons, which have been numbered. The sugar to its right is the same glucose, with all but one “C” removed. The other five carbons are still there but are inferred using the conventions of organic chemistry: Anywhere there is a corner, there’s a carbon unless otherwise indicated. It might be a good exercise for you to add in a “C” over each corner so that you gain a good understanding of this convention. You should end up adding in five carbon symbols; the sixth is already given because that is conventionally included when it occurs outside of the ring.
On the left is a glucose with all of its carbons indicated. They’re also numbered, which is important to understand now for information that comes later. On the right is the same molecule, glucose, without the carbons indicated (except for the sixth one). Wherever there is a corner, there is a carbon, unless otherwise indicated (as with the oxygen). On the bottom left is ribose, the sugar found in RNA. The sugar on the bottom right is deoxyribose. Note that at carbon 2 (*), the ribose and deoxyribose differ by a single oxygen.
The lower left sugar in the figure is a ribose. In this depiction, the carbons, except the one outside of the ring, have not been drawn in, and they are not numbered. This is the standard way sugars are presented in texts. Can you tell how many carbons there are in this sugar? Count the corners and don’t forget the one that’s already indicated!
If you said “five,” you are right. Ribose is a pentose (pent = five) and happens to be the sugar present in ribonucleic acid, or RNA. Think to yourself what the sugar might be in deoxyribonucleic acid, or DNA. If you thought, deoxyribose, you’d be right.
The fourth sugar given in the figure is a deoxyribose. In organic chemistry, it’s not enough to know that corners indicate carbons. Each carbon also has a specific number, which becomes important in discussions of nucleic acids. Luckily, we get to keep our carbon counting pretty simple in basic biology. To count carbons, you start with the carbon to the right of the non-carbon corner of the molecule. The deoxyribose or ribose always looks to me like a little cupcake with a cherry on top. The “cherry” is an oxygen. To the right of that oxygen, we start counting carbons, so that corner to the right of the “cherry” is the first carbon. Now, keep counting. Here’s a little test: What is hanging down from carbon 2 of the deoxyribose?
If you said a hydrogen (H), you are right! Now, compare the deoxyribose to the ribose. Do you see the difference in what hangs off of the carbon 2 of each sugar? You’ll see that the carbon 2 of ribose has an –OH, rather than an H. The reason the deoxyribose is called that is because the O on the second carbon of the ribose has been removed, leaving a “deoxyed” ribose. This tiny distinction between the sugars used in DNA and RNA is significant enough in biology that we use it to distinguish the two nucleic acids.
In fact, these subtle differences in sugars mean big differences for many biological molecules. Below, you’ll find a couple of ways that apparently small changes in a sugar molecule can mean big changes in what it does. These little changes make the difference between a delicious sugar cookie and the crunchy exoskeleton of a dung beetle.
Sugar and Fuel
A marathon runner keeps fuel on hand in the form of “carbs,” or sugars. These fuels provide the marathoner’s straining body with the energy it needs to keep the muscles pumping. When we take in sugar like this, it often comes in the form of glucose molecules attached together in a polymer called starch. We are especially equipped to start breaking off individual glucose molecules the minute we start chewing on a starch.
Double X Extra: A monomer is a building block (mono = one) and a polymer is a chain of monomers. With a few dozen monomers or building blocks, we get millions of different polymers. That may sound nutty until you think of the infinity of values that can be built using only the numbers 0 through 9 as building blocks or the intricate programming that is done using only a binary code of zeros and ones in different combinations.
Our bodies then can rapidly take the single molecules, or monomers, into cells and crack open the chemical bonds to transform the energy for use. The bonds of a sugar are packed with chemical energy that we capture to build a different kind of energy-containing molecule that our muscles access easily. Most species rely on this process of capturing energy from sugars and transforming it for specific purposes.
Polysaccharides: Fuel and Form
Plants use the Sun’s energy to make their own glucose, and starch is actually a plant’s way of storing up that sugar. Potatoes, for example, are quite good at packing away tons of glucose molecules and are known to dieticians as a “starchy” vegetable. The glucose molecules in starch are packed fairly closely together. A string of sugar molecules bonded together through dehydration synthesis, as they are in starch, is a polymer called a polysaccharide (poly = many; saccharide = sugar). When the monomers of the polysaccharide are released, as when our bodies break them up, the reaction that releases them is called hydrolysis.
Double X Extra: The specific reaction that hooks one monomer to another in a covalent bond is called dehydration synthesis because in making the bond–synthesizing the larger molecule–a molecule of water is removed (dehydration). The reverse is hydrolysis (hydro = water; lysis = breaking), which breaks the covalent bond by the addition of a molecule of water.
Although plants make their own glucose and animals acquire it by eating the plants, animals can also package away the glucose they eat for later use. Animals, including humans, store glucose in a polysaccharide called glycogen, which is more branched than starch. In us, we build this energy reserve primarily in the liver and access it when our glucose levels drop.
Whether starch or glycogen, the glucose molecules that are stored are bonded together so that all of the molecules are oriented the same way. If you view the sixth carbon of the glucose to be a “carbon flag,” you’ll see in the figure that all of the glucose molecules in starch are oriented with their carbon flags on the upper left.
The orientation of monomers of glucose in polysaccharides can make a big difference in the use of the polymer. The glucoses in the molecule on the top are all oriented “up” and form starch. The glucoses in the molecule on the bottom alternate orientation to form cellulose, which is quite different in its function from starch.
Storing up sugars for fuel and using them as fuel isn’t the end of the uses of sugar. In fact, sugars serve as structural molecules in a huge variety of organisms, including fungi, bacteria, plants, and insects.
The primary structural role of a sugar is as a component of the cell wall, giving the organism support against gravity. In plants, the familiar old glucose molecule serves as one building block of the plant cell wall, but with a catch: The molecules are oriented in an alternating up-down fashion. The resulting structural sugar is called cellulose.
That simple difference in orientation means the difference between a polysaccharide as fuel for us and a polysaccharide as structure. Insects take it step further with the polysaccharide that makes up their exoskeleton, or outer shell. Once again, the building block is glucose, arranged as it is in cellulose, in an alternating conformation. But in insects, each glucose has a little extra added on, a chemical group called an N-acetyl group. This addition of a single functional group alters the use of cellulose and turns it into a structural molecule that gives bugs that special crunchy sound when you accidentally…ahem…step on them.
These variations on the simple theme of a basic carbon-ring-as-building-block occur again and again in biological systems. In addition to serving roles in structure and as fuel, sugars also play a role in function. The attachment of subtly different sugar molecules to a protein or a lipid is one way cells communicate chemically with one another in refined, regulated interactions. It’s as though the cells talk with each other using a specialized, sugar-based vocabulary. Typically, cells display these sugary messages to the outside world, making them available to other cells that can recognize the molecular language.
Lipids: The Fatty Trifecta
Starch makes for good, accessible fuel, something that we immediately attack chemically and break up for quick energy. But fats are energy that we are supposed to bank away for a good long time and break out in times of deprivation. Like sugars, fats serve several purposes, including as a dense source of energy and as a universal structural component of cell membranes everywhere.
Fats: the Good, the Bad, the Neutral
Turn again to a nutrition label, and you’ll see a few references to fats, also known as lipids. (Fats are slightly less confusing that sugars in that they have only two names.) The label may break down fats into categories, including trans fats, saturated fats, unsaturated fats, and cholesterol. You may have learned that trans fats are “bad” and that there is good cholesterol and bad cholesterol, but what does it all mean?
Let’s start with what we mean when we say saturated fat. The question is, saturated with what? There is a specific kind of dietary fat call the triglyceride. As its name implies, it has a structural motif in which something is repeated three times. That something is a chain of carbons and hydrogens, hanging off in triplicate from a head made of glycerol, as the figure shows. Those three carbon-hydrogen chains, or fatty acids, are the “tri” in a triglyceride. Chains like this can be many carbons long.
Double X Extra: We call a fatty acid a fatty acid because it’s got a carboxylic acid attached to a fatty tail. A triglyceride consists of three of these fatty acids attached to a molecule called glycerol. Our dietary fat primarily consists of these triglycerides.
Triglycerides come in several forms. You may recall that carbon can form several different kinds of bonds, including single bonds, as with hydrogen, and double bonds, as with itself. A chain of carbon and hydrogens can have every single available carbon bond taken by a hydrogen in single covalent bond. This scenario of hydrogen saturation yields a saturated fat. The fat is saturated to its fullest with every covalent bond taken by hydrogens single bonded to the carbons.
Saturated fats have predictable characteristics. They lie flat easily and stick to each other, meaning that at room temperature, they form a dense solid. You will realize this if you find a little bit of fat on you to pinch. Does it feel pretty solid? That’s because animal fat is saturated fat. The fat on a steak is also solid at room temperature, and in fact, it takes a pretty high heat to loosen it up enough to become liquid. Animals are not the only organisms that produce saturated fat–avocados and coconuts also are known for their saturated fat content.
The top graphic above depicts a triglyceride with the glycerol, acid, and three hydrocarbon tails. The tails of this saturated fat, with every possible hydrogen space occupied, lie comparatively flat on one another, and this kind of fat is solid at room temperature. The fat on the bottom, however, is unsaturated, with bends or kinks wherever two carbons have double bonded, booting a couple of hydrogens and making this fat unsaturated, or lacking some hydrogens. Because of the space between the bumps, this fat is probably not solid at room temperature, but liquid.
You can probably now guess what an unsaturated fat is–one that has one or more hydrogens missing. Instead of single bonding with hydrogens at every available space, two or more carbons in an unsaturated fat chain will form a double bond with carbon, leaving no space for a hydrogen. Because some carbons in the chain share two pairs of electrons, they physically draw closer to one another than they do in a single bond. This tighter bonding result in a “kink” in the fatty acid chain.
In a fat with these kinks, the three fatty acids don’t lie as densely packed with each other as they do in a saturated fat. The kinks leave spaces between them. Thus, unsaturated fats are less dense than saturated fats and often will be liquid at room temperature. A good example of a liquid unsaturated fat at room temperature is canola oil.
A few decades ago, food scientists discovered that unsaturated fats could be resaturated or hydrogenated to behave more like saturated fats and have a longer shelf life. The process of hydrogenation–adding in hydrogens–yields trans fat. This kind of processed fat is now frowned upon and is being removed from many foods because of its associations with adverse health effects. If you check a food label and it lists among the ingredients “partially hydrogenated” oils, that can mean that the food contains trans fat.
Double X Extra: A triglyceride can have up to three different fatty acids attached to it. Canola oil, for example, consists primarily of oleic acid, linoleic acid, and linolenic acid, all of which are unsaturated fatty acids with 18 carbons in their chains.
Why do we take in fat anyway? Fat is a necessary nutrient for everything from our nervous systems to our circulatory health. It also, under appropriate conditions, is an excellent way to store up densely packaged energy for the times when stores are running low. We really can’t live very well without it.
Phospholipids: An Abundant Fat
You may have heard that oil and water don’t mix, and indeed, it is something you can observe for yourself. Drop a pat of butter–pure saturated fat–into a bowl of water and watch it just sit there. Even if you try mixing it with a spoon, it will just sit there. Now, drop a spoon of salt into the water and stir it a bit. The salt seems to vanish. You’ve just illustrated the difference between a water-fearing (hydrophobic) and a water-loving (hydrophilic) substance.
Generally speaking, compounds that have an unequal sharing of electrons (like ions or anything with a covalent bond between oxygen and hydrogen or nitrogen and hydrogen) will be hydrophilic. The reason is that a charge or an unequal electron sharing gives the molecule polarity that allows it to interact with water through hydrogen bonds. A fat, however, consists largely of hydrogen and carbon in those long chains. Carbon and hydrogen have roughly equivalent electronegativities, and their electron-sharing relationship is relatively nonpolar. Fat, lacking in polarity, doesn’t interact with water. As the butter demonstrated, it just sits there.
There is one exception to that little maxim about fat and water, and that exception is the phospholipid. This lipid has a special structure that makes it just right for the job it does: forming the membranes of cells. A phospholipid consists of a polar phosphate head–P and O don’t share equally–and a couple of nonpolar hydrocarbon tails, as the figure shows. If you look at the figure, you’ll see that one of the two tails has a little kick in it, thanks to a double bond between the two carbons there.
Phospholipids form a double layer and are the major structural components of cell membranes. Their bend, or kick, in one of the hydrocarbon tails helps ensure fluidity of the cell membrane. The molecules are bipolar, with hydrophilic heads for interacting with the internal and external watery environments of the cell and hydrophobic tails that help cell membranes behave as general security guards.
The kick and the bipolar (hydrophobic and hydrophilic) nature of the phospholipid make it the perfect molecule for building a cell membrane. A cell needs a watery outside to survive. It also needs a watery inside to survive. Thus, it must face the inside and outside worlds with something that interacts well with water. But it also must protect itself against unwanted intruders, providing a barrier that keeps unwanted things out and keeps necessary molecules in.
Phospholipids achieve it all. They assemble into a double layer around a cell but orient to allow interaction with the watery external and internal environments. On the layer facing the inside of the cell, the phospholipids orient their polar, hydrophilic heads to the watery inner environment and their tails away from it. On the layer to the outside of the cell, they do the same.
As the figure shows, the result is a double layer of phospholipids with each layer facing a polar, hydrophilic head to the watery environments. The tails of each layer face one another. They form a hydrophobic, fatty moat around a cell that serves as a general gatekeeper, much in the way that your skin does for you. Charged particles cannot simply slip across this fatty moat because they can’t interact with it. And to keep the fat fluid, one tail of each phospholipid has that little kick, giving the cell membrane a fluid, liquidy flow and keeping it from being solid and unforgiving at temperatures in which cells thrive.
Steroids: Here to Pump You Up?
Our final molecule in the lipid fatty trifecta is cholesterol. As you may have heard, there are a few different kinds of cholesterol, some of which we consider to be “good” and some of which is “bad.” The good cholesterol, high-density lipoprotein, or HDL, in part helps us out because it removes the bad cholesterol, low-density lipoprotein or LDL, from our blood. The presence of LDL is associated with inflammation of the lining of the blood vessels, which can lead to a variety of health problems.
But cholesterol has some other reasons for existing. One of its roles is in the maintenance of cell membrane fluidity. Cholesterol is inserted throughout the lipid bilayer and serves as a block to the fatty tails that might otherwise stick together and become a bit too solid.
Cholesterol’s other starring role as a lipid is as the starting molecule for a class of hormones we called steroids or steroid hormones. With a few snips here and additions there, cholesterol can be changed into the steroid hormones progesterone, testosterone, or estrogen. These molecules look quite similar, but they play very different roles in organisms. Testosterone, for example, generally masculinizes vertebrates (animals with backbones), while progesterone and estrogen play a role in regulating the ovulatory cycle.
Double X Extra: A hormone is a blood-borne signaling molecule. It can be lipid based, like testosterone, or short protein, like insulin.
As you progress through learning biology, one thing will become more and more clear: Most cells function primarily as protein factories. It may surprise you to learn that proteins, which we often talk about in terms of food intake, are the fundamental molecule of many of life’s processes. Enzymes, for example, form a single broad category of proteins, but there are millions of them, each one governing a small step in the molecular pathways that are required for living.
Levels of Structure
Amino acids are the building blocks of proteins. A few amino acids strung together is called a peptide, while many many peptides linked together form a polypeptide. When many amino acids strung together interact with each other to form a properly folded molecule, we call that molecule a protein.
For a string of amino acids to ultimately fold up into an active protein, they must first be assembled in the correct order. The code for their assembly lies in the DNA, but once that code has been read and the amino acid chain built, we call that simple, unfolded chain the primary structure of the protein.
This chain can consist of hundreds of amino acids that interact all along the sequence. Some amino acids are hydrophobic and some are hydrophilic. In this context, like interacts best with like, so the hydrophobic amino acids will interact with one another, and the hydrophilic amino acids will interact together. As these contacts occur along the string of molecules, different conformations will arise in different parts of the chain. We call these different conformations along the amino acid chain the protein’s secondary structure.
Once those interactions have occurred, the protein can fold into its final, or tertiary structure and be ready to serve as an active participant in cellular processes. To achieve the tertiary structure, the amino acid chain’s secondary interactions must usually be ongoing, and the pH, temperature, and salt balance must be just right to facilitate the folding. This tertiary folding takes place through interactions of the secondary structures along the different parts of the amino acid chain.
The final product is a properly folded protein. If we could see it with the naked eye, it might look a lot like a wadded up string of pearls, but that “wadded up” look is misleading. Protein folding is a carefully regulated process that is determined at its core by the amino acids in the chain: their hydrophobicity and hydrophilicity and how they interact together.
In many instances, however, a complete protein consists of more than one amino acid chain, and the complete protein has two or more interacting strings of amino acids. A good example is hemoglobin in red blood cells. Its job is to grab oxygen and deliver it to the body’s tissues. A complete hemoglobin protein consists of four separate amino acid chains all properly folded into their tertiary structures and interacting as a single unit. In cases like this involving two or more interacting amino acid chains, we say that the final protein has a quaternary structure. Some proteins can consist of as many as a dozen interacting chains, behaving as a single protein unit.
A Plethora of Purposes
What does a protein do? Let us count the ways. Really, that’s almost impossible because proteins do just about everything. Some of them tag things. Some of them destroy things. Some of them protect. Some mark cells as “self.” Some serve as structural materials, while others are highways or motors. They aid in communication, they operate as signaling molecules, they transfer molecules and cut them up, they interact with each other in complex, interrelated pathways to build things up and break things down. They regulate genes and package DNA, and they regulate and package each other.
As described above, proteins are the final folded arrangement of a string of amino acids. One way we obtain these building blocks for the millions of proteins our bodies make is through our diet. You may hear about foods that are high in protein or people eating high-protein diets to build muscle. When we take in those proteins, we can break them apart and use the amino acids that make them up to build proteins of our own.
How does a cell know which proteins to make? It has a code for building them, one that is especially guarded in a cellular vault in our cells called the nucleus. This code is deoxyribonucleic acid, or DNA. The cell makes a copy of this code and send it out to specialized structures that read it and build proteins based on what they read. As with any code, a typo–a mutation–can result in a message that doesn’t make as much sense. When the code gets changed, sometimes, the protein that the cell builds using that code will be changed, too.
Biohazard!The names associated with nucleic acids can be confusing because they all start with nucle-. It may seem obvious or easy now, but a brain freeze on a test could mix you up. You need to fix in your mind that the shorter term (10 letters, four syllables), nucleotide, refers to the smaller molecule, the three-part building block. The longer term (12 characters, including the space, and five syllables), nucleic acid, which is inherent in the names DNA and RNA, designates the big, long molecule.
DNA vs. RNA: A Matter of Structure
DNA and its nucleic acid cousin, ribonucleic acid, or RNA, are both made of the same kinds of building blocks. These building blocks are called nucleotides. Each nucleotide consists of three parts: a sugar (ribose for RNA and deoxyribose for DNA), a phosphate, and a nitrogenous base. In DNA, every nucleotide has identical sugars and phosphates, and in RNA, the sugar and phosphate are also the same for every nucleotide.
So what’s different? The nitrogenous bases. DNA has a set of four to use as its coding alphabet. These are the purines, adenine and guanine, and the pyrimidines, thymine and cytosine. The nucleotides are abbreviated by their initial letters as A, G, T, and C. From variations in the arrangement and number of these four molecules, all of the diversity of life arises. Just four different types of the nucleotide building blocks, and we have you, bacteria, wombats, and blue whales.
RNA is also basic at its core, consisting of only four different nucleotides. In fact, it uses three of the same nitrogenous bases as DNA–A, G, and C–but it substitutes a base called uracil (U) where DNA uses thymine. Uracil is a pyrimidine.
DNA vs. RNA: Function Wars
An interesting thing about the nitrogenous bases of the nucleotides is that they pair with each other, using hydrogen bonds, in a predictable way. An adenine will almost always bond with a thymine in DNA or a uracil in RNA, and cytosine and guanine will almost always bond with each other. This pairing capacity allows the cell to use a sequence of DNA and build either a new DNA sequence, using the old one as a template, or build an RNA sequence to make a copy of the DNA.
These two different uses of A-T/U and C-G base pairing serve two different purposes. DNA is copied into DNA usually when a cell is preparing to divide and needs two complete sets of DNA for the new cells. DNA is copied into RNA when the cell needs to send the code out of the vault so proteins can be built. The DNA stays safely where it belongs.
RNA is really a nucleic acid jack-of-all-trades. It not only serves as the copy of the DNA but also is the main component of the two types of cellular workers that read that copy and build proteins from it. At one point in this process, the three types of RNA come together in protein assembly to make sure the job is done right.
The Cell Motion BioBus, ready to be boarded by all interested parties. And I do mean parties
About two years ago, I received one of those university-wide mass emails aimed to solicit scientist volunteers to help teach science at an underprivileged school in Manhattan. Given my interest in science education and communication, I read on. The request was on behalf of something called the Cell Motion BioBus, which is a 1974 San Francisco transit bus that has been converted into a high-tech mobile microscopy lab, and for that particular day, the duties of the scientist volunteer involved teaching 3rd graders about the tiny crustacean,Daphnia.
A few weeks later, I found myself inside The BioBus, hanging out and talking science with a bunch of very excited 8-year-olds. We spoke about the habitat whereDaphnia lives, the food it eats, and how it reproduces. We examinedDaphnia anatomy using diagrams on the computer, being sure to locate the heart. After this lesson, the kids went on to mount realDaphnia samples onto microscope slides so that they can look at these tiny “water fleas” at high magnification. The kids did not hold back with their enthusiasm, laughing and giggling while pointing outDaphnia legs, antennae, and the beating heart. It was such a wonderful experience that I wrote about it.
Watching their faces light up with wonder and amazement over something so simple was incredibly gratifying for me, and I immediately came to understand why Dr. Ben, a Columbia University-bred PhD physicist, turned down several coveted offers to become an academic lab head. He, along with Sarah Weisberg, is currently fulfilling the dream of bringing science education to often-overlooked communities. However, as with many a good initiative, funding is limited.
To help keep The BioBus afloat, we at Double X Science are profiling this organization in our new series Good Deeds, Good Science. The timing couldn’t be more perfect because The BioBus is currently looking for help to get home after spreading some sciencey goodness to schools in Illinois, Kansas, Colorado, New Mexico, and Texas. Here is a letter from Sarah:
Dear Science Fan:
I am writing to tell you about a great non-profit organization I’ve been volunteering with, called the Cell Motion BioBus. The BioBus brings practicing scientists (graduate level and above) to teach K-12 students aboard their mobile lab — a converted 1974 transit bus that now houses a research-level microscope lab. I myself have seen how students of all ages and backgrounds respond to the BioBus, and it’s usually along the lines of, “That was AWESOME!”
The BioBus is also an amazing story of grassroots fundraising and charitable giving: the lab was built using donated equipment and labor and right now, the BioBus is at the end of a cross-country tour, during which it was able to bring research-level science to schools in places like rural Kansas, funded by small donations from its supporters.
Now, the BioBus needs help finishing its fundraising campaign so it can return to NYC and continue teaching in 2012. Please help by visiting www.fundly.com/biobus and giving what you can — this is grassroots work, and any amount helps!
Thanks so much, and Happy New Year!
Below is are a few videos of The BioBus trip thus far, which you can find on The BioBus YouTube Channel. If you are willing and able,please donate to this cause. Putting a science-induced smile on a kids face will be well worth it!
Jennifer Canale is a Senior Microbiologist for the United States Food and Drug Administration (FDA) in Queens, NY, as well as an adjunct microbiology lecturer for City University of NY (York College and College of Staten Island). Jennifer is also passionate about promoting women in science and leads an annual women in science event at the FDA as a means to promote awareness about gender discrimination in the workplace. [DXS] First, can you give me a quick overview of what your scientific background is and your current connection to science?
[JC] I have always been interested in science, and since most of my family worked in Bellvue Hospital, I was very comfortable around people in lab coats. In the early seventies, at the age of 5, I announced to my grandfather, the X-ray technician, and his brothers (my great uncles) that I wanted to become a doctor, specifically a doctor that delivers babies.
My grandfather was proud and my uncles were dismayed. My uncle Joe said to me, “Jennifer, you mean a nurse like your cousin Joanie, right?” My cousin Joan applied to Medical School in the sixties and the same group of uncles convinced her that her fiancé, Warren, wouldn’t wait 4 years to get married and it was more lady-like to be a nurse. Today she is a retired left-handed OR nurse that specializes in cracking open chests for cardiac surgery, not so lady-like after all. So in an attempt to not have a repeat of Joanie, my grandfather jumped to my defense against his brothers and said that ‘she can be a doctor if she wanted to be’, and, furthermore, his niece Joanie was smarter and more capable than most of the doctors he worked with and shouldn’t have had to take orders from them.
My uncles agreed that there was no question of the intellectual prowess possessed by both Joanie and myself, and their reluctance came out of concern for me. They worked in the hospital, too, and saw how male doctors would abuse the female ones and make their lives more difficult because they didn’t want to allow girls in the all-boys club. “Do you want our baby – our most precious blood – to have to fight her whole life for this? What about the family – how will she find a husband and bring us more children if she sticks her nose in a book the rest of her life?” These arguments sounded a lot better when they were stated in Sicilian. Back then, the concept of ‘women can have it all’ – work and family – was not the norm like it is today.
My grandfather came back with his final answers to them. I was his granddaughter, I looked just like him, I was a fighter just like him, and this is America and she will be what she wants to be, ‘End of Story’. My uncles agreed that I was his granddaughter, I looked just like him, and I was a stubborn mule just like him, so he was probably right and they would pray for me and secretly hope I would change my mind.
Now this all transpired in front of me in a combination of English and Sicilian while I stood there in my denim overalls with a Tweety Bird patch. I was listening, and since I was only beginning to learn Sicilian, I only caught a couple of words: blood, children, book, change, and I misunderstood the word for fighter as “afraid.” I added to my grandfather’s “end of story” remark that I was not afraid of blood, I can learn how to deliver children from a book, and questioned why they wanted me to change- those overalls were my favorite!
My family was supportive to a point, but when I asked for an erector set for Christmas, I got a Barbie town house. When I wanted to go camping with the Girl Scouts, I was sent to dance school (but, much to my amazement, I enjoyed that until I was 17). My parents started giving in around 3rdgrade, and I got the panda bear-shaped calculator I wanted, as well as the robot toy 2XL featuring the 8-track tape. My mom would beg me to watch Little House On the Prairie, but I preferred Star Trek (the original Kirk version), Lost in Space (Danger Will Robinson), and Land of the Lost. Of course this was all my dad’s fault according to mom – he was the sci-fi guy, but he always said, “Jen was born this way!”
My parents eventually gave up, and my uncles kept praying for that change of mind, but I spent the late seventies and early eighties winning science fairs with experiments my Uncle Ben, the electrician, rigged for me. They thought there was hope for me to be more “lady-like” in 1984 when I started high school and wanted to try out for the cheerleading squad, but the teachers advised me that “the cheer squad” was no place for an “honor student” like me. So it was off to advanced placement Biology and Chemistry, and by graduation in 1988, I was accepted to the pre-med program at NYU.
I graduated from NYU with honors, and my parents got me two presents: my name in diamonds and a stethoscope. My grandfather bought me a set of crisp white lab coats and gloated to his brothers with a cigar in his mouth. Apparently a bet was made amongst them and from hence forward they had to call me “doctoressa,” the hybrid feminized version of doctor in Italian.
The NYU pre-med was highly competitive – a constant process of elimination from 500 students (1:3, female:male) down to only 109 of us actually completing the program. The men thought it was strategic to flirt with the girls and convince us that we shouldn’t become doctors but instead should marry them. The guy that told me that got a punch in the stomach – in the name of the other women that worked. It was also apparent that many were planting the seeds of doubt in the pre-med females, stating that if we became doctors, then we wouldn’t be able to have a family. In essence, we were being told that we would be giving up the chance to have children. You had to go against your “true female nature” to breed and nurture and (instead) become a selfish and testosterone-like human to make it in this field. That was the nail in the coffin for a lot of the women in my program. The most brutal tactic and final blow to confidence was when I heard someone say that “only the ugly girls become doctors because no man would want them.”
In the nineties – halfway through college – I did change my mind, and my uncles were dancing in the streets. They thought I met a nice boy in college and I was going to settle down, give them more kids, and make sauce and meatballs on a Sunday like the good Paesana I was supposed to be. I announced I didn’t want to be an MD anymore, I wanted to be a PhD, instead. I wanted to be a SCIENTIST, do research, and maybe teach in a university. A “Scientista”-“Professoressa” “Aiuta Dio” (which means help us god)! Back to church and the rosary beads. When I got my master’s degree in microbiology, the family was just convinced I liked to collect graduation hats.
There was a feeling among my family members that science was a “boy thing,” and my cousins teased me as a result. They considered me a nerd and less feminine than my other girl cousins. I was told that I would never get married and have kids because I am a bookworm. Even in the mid-’90s, I had friends that told me not to tell guys that I was a scientist because they wouldn’t ask me out. I was kind of cute and only told a guy the truth about my profession if we got serious. As an experiment, I told one guy I met that I was a scientist and he said I looked too sexy to be that smart – and then he walked away.
I met discrimination on both sides of the stereotypical coin, in academia and in the work force. I was told when I was interviewing for graduate schools (and then for science jobs) that I had several strikes against me. First, strike one, my thick Staten Island/ Brooklyn accent supposedly made me sound less intelligent. My mentor in graduate school, Dr. Mark Albano, said to tell people to kiss your “you know what” because as long as I could discuss topics like “molecular genetics” who cares how it sounds. Besides he found my accent endearing, especially because it made boring topics sound more interesting.
Strike two was my long hair. I was told that my long hair was not practical in a scientific environment, and if I looked too glamorous on interviews I would not be taken seriously. I put my hair in a bun and toned down my make-up, but I didn’t cut it. Apparently, I looked too feminine, especially given my major curves, and even my power suits could not hide that. Women at the time were dressing very masculine (think early Miranda on Sex in the City) to compete with men for jobs. When I got the interview for my first job with Dr. Moretti in the Reproductive Immunology Lab at St. Vincent’s Medical Center in Staten Island, I remember wearing a black and white houndstooth print sheath dress with a matching short suit jacket, accessorized with pearls. Dr. Moretti said I was like Rosalind Franklin and Jackie Kennedy all rolled up into one, with a side order of cannoli.
The early 2000s arrived, and attitudes toward science changed. Shows like CSI became wildly popular. Science fiction movies about transforming robots became blockbusters. People began to use technology in their everyday lives, such as smart phones, tablets, and car navigation systems, and it suddenly became “cool.” I met my husband in 1999, and since I really was into him, I told him the truth about being a “microbiologist” from the start. He said, and I quote, “Wow, your smart, sexy, and Sicilian – it’s like I hit the Lotto!”
My wedding was the most joyful event in our family’s history because most of them thought that would never happen. I still get teased by my family when I give a long, drawn out scientific explanation of something or when I bake and make exact measurements of ingredients with my Pyrex bakeware with both the ounces and metric conversions. My husband responds for me and says “he learns something new everyday and hopes that our son becomes a nerd just like his mommy.”
So now I have it all: I am a female scientist, a wife, and a mother, even though others didn’t think that would be possible. But I always knew it would happen. I understood and forgave my uncles because I knew that they wanted to protect me, not hinder me. As for all my doubters I regularly take Dr. Albano’s advise and tell them to kiss my “you know what!”
Even my current supervisor, Maureen Coakley, recently told me in an interview that I am an “anomaly,” meaning that I am a flamboyant scientist. That was one of the best compliments I ever received. I am who I am, and that is why my playlist on my iPhone has the “Big Bang Theory Theme Song” followed by “I’m sexy and I know it!”
Times have changed. Perceptions have altered in a good way, but not entirely. Lesson learned from both academia and the school of life is that some people will get you and some people won’t. If they don’t, don’t take it personally because it is their loss and their ignorance. Some people see the person, and some see the stereotype. All you can do is try to educate them in an attempt to bust the stereotype. The only perception that matters is how you perceive yourself and use that perception as a means to become the woman that you were meant to be.
[DXS] What ways do you express yourself creatively that may not have a single thing to do with science?
[JC]Ever since planning my wedding in 2004, I have been interested in event planning. I have a knack at coordinating events, which I do as part of my collateral duties at FDA, where I have served as the Women’s Program Coordinator for the past 9 years. People call me the ”Fun Fairy” because I can be very creative and take any topic, put a different and interesting spin on it, and present it to a group in very entertaining ways. My creativity is driven by my intellectualism, and I incorporate that into something fun and memorable. I always make little inexpensive favors – buy them to give out to my audience – that are”theme oriented,” and they keep them as a reminder of the event.
The people I work with have whole collections of these favors, and they remember what each one stands for. For instance, the Women’s History Month theme for one year was “Our History is Our Strength.” Before planning this event, I had attended at NYU the Satellite Summit of National Women’s Conference hosted by Maria Shriver (then 1st Lady of California) and the First Lady, Michelle Obama. So I thought I would highlight the contributions of the First Ladies to US history. I found an educational video on the history of the First Ladies, did a presentation on the Satellite Summit, and even had a fashion show featuring of reproductions of Jacqueline Kennedy jewelry collection (my favorite first lady). I used the symbol of a “Cameo” to represent the first ladies, and so I made a huge paper one with beads on tulle on my bulletin board with pictures of the first ladies around it and gave out cameo bracelets that I made from gluing plastic cameo buttons on ribbon. Everyone still has a cameo on their desk at work, occasionally conjuring up memories of my First Ladies event.
[DXS] Do you find that your scientific background informs your creativity, even though what you do may not specifically be scientific?
[JC]My entire life is influenced by, or even revolves around, “Science.” I love science fiction movies, books, comic books, etc. Any inspiration I get for any of my creative projects always has some root in something “science-related.” I also think that my background in science helps make my visions come to life. Even the smallest details like the stemware I chose for my wedding was a Mikasa pattern that resembled a DNA double helix, or a hexagonal candleholder that looked like a benzene ring (at least it did to me!). Another example comes from my Women’s Program, when the theme was “Writing Women Back Into History.” So I found a book called The Women of Apollo, which gave the untold story of the women engineers who had critical contributions to the Apollo Space programs. For me, all roads lead back to science.
[DXS] Have you encountered situations in which your expression of yourself outside the bounds of science has led to people viewing you differently–either more positively or more negatively?
[JC]I have experienced both negative and positive views by others when I am expressing my self creatively. On one hand, there were people that associate planning events with a negative stereotype of being a “party-girl” or “bimbo” type that cares more about the “girly fun” stuff than the serious business of science. On the other hand, there have been people who constantly praise me for presenting science-related topics in entertaining ways. The latter view me as a “flamboyant scientist” who shares her knowledge in an interesting manner. In this life you will never please everyone; only seek to please yourself and your loved ones because those are the only opinions that matter.
[DXS] Have you found that your non-science expression of creativity/activity/etc. has in any way informed your understanding of science or how you may talk about it or present it to others?
[JC]In planning these events, I have come up with a formula of sorts to create a successful soirée. Of course, this formula is an entire science in itself. I have to consider things like timing, lighting, printed materials (programs, table cards, menus, etc.) and a gamut of other things that involve an understanding of science. I am a biologist with a minor in chemistry, but the more I do these events, the more I get into things like astronomy (for a celestial-themed wedding, for instance). I mention lighting, which seems so simple, because it is actually quite complicated – getting the right reflections and materials to use (i.e.- LEDs, wax candles vs. battery operated, the limitations of pyrotechnics in party venues) is critical. Even in doing crafts for favors and printed materials, like event programs, I’ve learned different scientific techniques, such the right kind of bonding agent to use to attach ribbons, charms, or vinyl decorations, or even the use of edible ink in printers to make fondant or wafer decorations to put on cupcakes or cakes. It is a continuous learning experience.
[DXS] How comfortable are you expressing your femininity and in what ways? How does this expression influence people’s perception of you in, say, a scientifically oriented context?
[JC]I am comfortable with expressing my femininity in the way I dress and conduct myself in any setting. Although, many years ago, I was advised to dress in suits and tailored shirts similar to a man and wear neutral make-up or none at all if I wanted to be taken seriously in the scientific world, I went against the grain. I am a curvy girl, and there is no hiding my femininity. So I embrace it. I wore suits, but nothing drab – always something like a red or purple skirt suit with heels. I adhere to work environment rules like no open toe shoes in the lab, which is a safety concern, but I do not downplay my female attributes to fit in, or to present a more palatable image to my scientific peers. I do not concern myself with people’s perceptions of me based on my looks because once I “speak” and “communicate” scientific concepts, there is no question of my prowess. I am what I am, and that is a female scientist, and I pride myself in being a “stereotype buster.”
[DXS] Do you think that the combination of your non-science creativity and scientific-related activity shifts people’s perspectives or ideas about what a scientist or science communicator is? If you’re aware of such an influence, in what way, if any, do you use it to (for example) reach a different corner of your audience or present science in a different sort of way?
[JC]I think that being the “flamboyant scientist” works in my favor, and as a science communicator, it is effective all aspects of my life. As an adjunct professor, my students often thank me for making science fun and understandable. As a scientist, my colleagues and interns find my training methods to be memorable and actually increase their understanding of the job. As the Women’s Program Coordinator at the FDA, I create unforgettable events that people look forward to and learn a lot from. As a wife, mother, daughter, aunt, cousin, and friend, I am the “Fun Fairy” (pictured with wings and a lab coat), and their lovable nerdy girl.
I feel my true gift is being able to communicate science. My mentor in graduate school always told me I had the talent of taking complicated scientific ideas and expressing them in a way that anyone could understand. I have some ideas brewing involving science books for children and teens, and I would like to explore these avenues in order to share this gift with others. I would also like to get involved in maybe writing for popular science publications, if given the opportunity.
[DXS] If you had something you could say to the younger you about the role of expression and creativity in your chosen career path, what would you say?
[JC]I would say be true to yourself. Whatever path you take career-wise, always remember that is could be something you will be doing the rest of your life. Yes, there are financial considerations to make, but if you do not have that creative outlet incorporated into your career, then you will be miserable. I am the happiest at work when I am planning a Women’s Program alongside doing experiments or going to my second job as a professor at York College. You need the creativity to keep the blood flowing. Where would science be without creativity? Find what your talent is and what makes you happy, and then apply it to your career. That is the secret to success.