Double X Science panel at GeekGirlCon 2012

On Sunday, Aug 12, Managing Editor Emily Willingham, Chemistry Editor Adrienne Roehrich, and Contributor Raychelle Burks spoke on bringing science to you. Here’s a summary of our panel.

Photo by Ryan Roehrich and used with permission.

We started with a welcome and gratitude to the organizers and attendees and our tagline “Science, I am Just That Into You.” We were selected to appear with a lot of fantastic programming over the weekend.
We introduced our 3 panelists:
Adrienne Roehrich, your panel moderator and the chemistry editor at Double X Science
Emily Willingham, founder and managing editor 
Ray Burks, contributor to Double X Science 
Photo by Ryan Roehrich and used with permission.

All 3 have PhDs in their respective fields – Emily is a developmental biologist, Ray is an analytical chemist, and Adrienne is a physical chemist. Emily and Ray are prolific writers. You can find their articles all over the internet and in print. Ray is a staff member for GeekGirlCon and Adrienne is a Special Agent volunteer. All 3 are active on social media and welcome live-tweeting and suggest the #DXS hashtag along with the #GGC12. And you can use the @DoubleXSci for the panel.

Then a poll of the room to see who had heard of the site. Only a few attendees were already familiar with the site, so we told them that DoubleXScience covers a lot of current science. For example on (the previous) Monday, Emily posted about the Mars Curiosity Rover touchdown. In July, the physics editor covered the Higgs particle announcement. We also cover timeless, yet updated science, such as pregnancy and other health issues that we editors perceive to be of interest to ourselves and our readers.
It’s hard to discuss what Double X Science is without discussing who it is.
After a review of who all the people on that particular slide are and what they have to do with Double X Science, three questions were asked by the moderator:
In November of 2011, Emily founded Double X Science, Emily what was your motivation in founding the site and what was then and is now your vision for it?
As mentioned, we have content from editors, other sites and contributors. Ray was the first contributor to the site – what attracted you to Double X Science?
What do the attendees want to know?
And then our discussion really got started. Thankfully, we had 3 great tweeters attending, so I can just point you along their tweets:

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Photo by Adrienne Roehrich and used with permission.

Posted by Adrienne M. Roehrich, Chemistry Editor

100 Years

By Adrienne M. Roehrich, Chemistry Editor

Photo of the author with her 100 year old grandmother 10-1-2012

100 is such a nice round number. 

Should I start with a disclaimer? I’m a chemist, not a biologist. Perhaps I should leave a post on centenarians to the biologists, but I have a vested interest in the topic. On October 1 of this year, my grandmother turned 100, so I’ve been a little obsessed with living until 100. In the United States, an estimated 1 in 4400 people reach the age of 100 and the highest number worldwide. The next highest number of centenarians reside in Japan, with a rate of 1 in 3500 people. 

The question is, why do these people live so long? This is a highly studied question. When one delves into the literature, as with most questions, there is no simple answer and often studies conflict with each other. There are different modes of study: some scientists study those who have become centenarians to try to determine what they have done to reach this rare milestone while other scientists work in theories, then animal models to study what pathways lead to longevity.

Studies have found that healthy centenarians in some areas have high levels of vitamin A and vitamin E1 and higher red blood cell glutathione reductase and catalase activities.2,3 But the presence of higher levels of these vitamins and glutathione reductase is not present in all centenarians, and the mere presence of these high levels does not necessarily indicate longevity.

 

Molecules that may or may not help longevity

You may have heard exclamations about antioxidants or calorie restriction. While antioxidants (the aforementioned vitamin A and vitamin E) are known to protect the body from the harmful effects of free-radicals, which occur in the normal processes of the body, evidence does not support that simply adding more antioxidants to the diet will slow aging. There are studies also showing that calorie restriction may have beneficial effects in terms of markers of aging in some animals, but many animals that are commonly used as human models do not extend longevity under calorie restriction, and such a course of action may have deleterious effects. The safety and benefits of long-term calorie restriction is currently unknown. Scientists are working towards answering these questions. 

Genetics plays an important role. The best predictor of a person reaching 100 is having a sibling live past 100. Variations in genes abound, but other than children of long-lived parents living longer, specifics are elusive. Oddly, being born in the Fall (September through November) is linked with a higher likelihood of becoming a centenarian.4 And functional independence for a longer period of time (past the age of 90) was found to be strongly correlated to centenarians. 90% of the participants in the New England Centenarian study were found to have been so.

Hormones are integral to our body function and have been studied for their potential pathways in longevity. Testosterone has been focused on, and lately a study of Korean eunuchs gave a higher rate of centenarians, 3 in 81 individuals. Due to the wide variability of the amount of testosterone produced by individuals, whether more or less testosterone exposure is beneficial or deleterious is unknown. 

What causes aging? This question is so important the National Institutes of Health (NIH) has devoted National Institute on Aging, the leading research institute on aging. A summary in more detail than I have gone into here is given on the NIH NIA’s site about preventing aging

If we look at the cellular level, scientists discovered that complete copying of DNA is dictated by telomeres and the enzyme telomerase, which earned 3 scientists the Nobel Prize in Physiology and Medicine in 2009. The unique DNA sequence in the telomeres protects chromosomes from degradation. When telomeres are shortened, cells age. Eventually, the telomeres will shorten, and cells will age and die. Unfortunately, extending telomeres or increasing the activity of telomerase enzyme does not help anti-aging, it contributes towards the growth of cancerous cells. 

A conversation with Dr. Mark D Johnson on twitter gave me these neat facts: Complete natural Homo sapiens LifeSpan = 120 years! All mammals except humans, bonobos, and chimpanzees, live six times their growth cycle. We grow within 20 years. That means natural mammal lifespan of 120. 

Overall, the contributing factors towards ageing and longevity are deemed to be complicated and there is no short-order anti-aging remedy.

Turning more towards my own field of expertise, the Maillard Reaction, a chemical reaction that makes cooked food tasty, also turns 100. Obviously, the actual chemical reaction goes back longer than 100 years – to when amino acids began to react with sugars at elevated temperatures. However, the French chemist Louis-Camille Maillard first reported the nature of these reactions in 1912.5 Maillard chemistry not only describes the molecules in baked bread, grilled veggies, and brewing of beer, but also other molecules as products, so many that chemists did not study Maillard chemistry in detail until World War II. Nearly 60 years ago, African American chemist John E. Hodge reported a mechanism for the Maillard reaction6

Hodge’s Flowchart of the Maillard Reaction
Products of the Maillard reaction range from molecules that are both welcome and abhorrent. The usually enjoyed flavor and aroma of roasted coffee is a product of the Maillard reaction, as is the char on the surface of grilled food which is considered to be carcinogenic. 

Roasted Coffee Beans, photo by Adrienne Roehrich
Grilled Yams, photo by Adrienne Roehrich

Do you know someone or something that has reached the anniversary of 100 years on this earth? 


References:
(1) Mecocci, P.; Polidori, M. C.; Troiano, L.; Cherubini, A.; Cecchetti, R.; Pini, G.; Straatman, M.; Monti, D.; Stahl, W.; Sies, H.; Franceschi, C.; Senin, U. Free Radical Biology and Medicine 2000, 28, 1243.
(2) Klapcinska, B.; Derejczyk, J.; Wieczorowska-Tobis, K.; Sobczak, A.; Sadowska-Krepa, E.; Danch, A. Acta Biochimica Ponoica 2000, 47, 281.
(3) Andersen, H. R.; Jeune, B.; Nybo, H.; Neilsen, J. B.; Andersen-Randberg, K.; Grandjean, P. Age and Ageing 1998, 27, 643.
(4) Journal of Aging Research 2011, 2011.
(5) Maillard, L.-C. Comp. Rend. 1912, 66.
(6) Hodge, J. E. Journal of Agricultural and Food Chemistry 1953, 1, 928.

Biology Explainer: The big 4 building blocks of life–carbohydrates, fats, proteins, and nucleic acids

The short version
  • 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.
Carbohydrates

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.

Proteins

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.

Nucleic Acids

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.


 By Emily Willingham, DXS managing editor 
This material originally appeared in similar form in Emily Willingham’s Complete Idiot’s Guide to College Biology

From alchemist to chemist: What kind of chemistry is that?


Figure 1: The Alchemist Discovering Phosphorus

What does the word chemistry  mean to you? For many, it was a class in high school or college to get through. In these introductory courses, called general chemistry, one gets a mix of all the flavors of chemistry – but the flavors are very different. To those who hear the calling of chemistry, it isn’t just any chemistry that will do. Some courses are more interesting to them than others. 

Many instructors start their general chemistry course with a history, introducing alchemy. Alchemy is considered to be the process by which to turn [name item of your choice] into gold. Alchemists were chemists by accident in that they performed many chemical reactions in their quests, discovering a number of elements in the process - embodied by Hennig Brandt’s discovery of phosphorus from the refinement of urine.
Alchemy relates to all the fields of chemistry. In perhaps the most famous of alchemy pictures, that by Joseph Wright of Derby entitled “The Alchemist Discovering Phosphorus,” the alchemist is kneeling by a very large round bottom flask. For many in modern chemistry, the round bottom flask signifies hours in the organic chemistrylaboratory mixing chemicals together to create something new.


Organic chemistry is the “branch of chemistry that deals with the structure, properties, and reactions of compounds that contain carbon” according to the American Chemical Association (ACS). Organic chemistry is the largest of chemistry fields in terms of number of people working in it. Organic chemists strive to make new compounds, usually to improve upon an existing one for a purpose and the field is often thought of in terms of synthesis applications.


The actual process of converting urine to phosphorus generally falls along the lines of inorganic chemical reactions. The form of phosphorus in urine is in the chemical sodium phosphate (Na3PO43-). Heating phosphates along with the organic products also in urine will form carbon monoxide (CO) and elemental phosphorus (P). The sodium phosphate, carbon monoxide, and elemental phosphate are all inorganic chemicals, falling under the field of inorganic chemistry.


Inorganic chemistry is “concerned with the properties and reactivity of all chemical elements,” according to UC-Davis chemwiki. While organic chemistry requires the presence of carbon in a specific type of bond, inorganic chemistry involves all the elements present in the periodic table. Inorganic chemistry delves into theories surrounding the bonding of metals to molecules and the shapes of molecules themselves.


Figure 2: Components of Urine
While the process of collecting phosphorus from urine requires organic and inorganic chemical reactions, the process of making the products in urine is biochemistry. Note in figure 2 that the primary product in urine is urea.


For students of biochemistry, images of the urea cycle (aka the Krebs cycle) are well known. According to the ACS, biochemistry is “the study of the structure, composition, and chemical reactions of substances in living systems.” Besides the chemical cycles to produce and use up necessary chemicals in biology, biochemistry encompasses protein structure and function (including enzymes), nucleic acids such as DNA, and biosynthesis.


As the alchemist turned urine to phosphorus, he added heat. The addition of heat to a reaction involves thermodynamics, a subsection of physical chemistry. If heat hadn’t been added, the reaction products would have been kinetic, which is another subsection of physical chemistry.


In a suite of physical chemistry courses, a student would also take quantum mechanics, rounding out the aim of physical chemists, which is to “develop a fundamental understanding at the molecular and atomic level of how materials behave and how chemical reactions occur,” according to the ACS. Physical chemists work by applying physics and math to the problems that chemists, biologists, and engineers study.


The alchemists who took exact measurements of their reactants and products, using quantitative methods, employed analytical chemistry. Presumably, the alchemists did this because every ounce of gold was precious, and they wanted to know how much substance they started with to produce the coveted metal.


Analytical chemistry focuses on obtaining and processing information about the composition and structure of matter. There are so-called wet lab ways to determine these quantities that often been employed. However, most analytical labs consist of the precision instrumentation that you may have seen on forensic crime shows, such as a mass spec, short for mass spectrometer, a frequent player on CSI.


While the alchemists were only trying to produce a substance to enrich pockets, they ultimately led to a rich science with several subfields, each with a trail leading from the practice of alchemy.

Adrienne M Roehrich, Double X Science Chemistry Editor
References:

(1734-1797), Joseph Wright of Derby. “English: The Alchemist Discovering Phosphorus or the Alchemist in Search of the Philosophers Stone.” Derby Museum and Art Gallery, Derby, U.K., 1771.

Lawton, Graham. “Pee-Cycling.” New Scientist, 20 December 2006 2006.

Weeks, Mary Elvira. “The Discovery of the Elements. Xxi. Supplementary Note on the Discovery of Phosphorus.” Journal of Chemical Education 10, no. 5 (1933/05/01 1933): 302.

Historical Physicists

Featured today are 10 more women who broke boundaries by their presence in physics. They lived from 1711 to 2000. While I again limited information to one paragraph, I tried to highlight how they got their start, what universities, family members, and scientists were supportive of them. For these women, without the support of fathers, mothers, husbands, and mentors (all male with one exception) their life in science would not have happened. While barriers are not as difficult today as they were at the times these women made their way, it is a testament to what can be done when families and scientists support each other. These women are an inspiration and I hope you look up more information for them. In addition, I’d love to hear who your favorite women in science are in the comments.

Laura Bassi by Carlo Vandi 
Laura Bassi (1711-78) lectured on science until a few hoursbefore her death. An Italian scientist of international fame and one of the first women physicists in western history, Dr. Bassi earned her doctorate in philosophy and science through public debate from the University of Bologna. The University of Bologna offered Dr. Bassi a position in an effort to be known as a leader in women’s education. Unfortunately, this forward step was not acceptable to much of the rest of the world’s academic community and required stipulations to Dr. Bassi teaching. However, she countered these limitations with determination and passion. Her appointment to full membership in the Bendettini Academics also deterred some naysayers of Dr. Bassi’s involvement in research and teaching. In order to further her career, she married. A married woman could achieve more than a single woman at that time. Her death in 1778 was unexpected, especially as she had participated in an Academy of Sciences lecture on a few hours before.



If you can access the full article, I highly recommend The Desire to Contribute: AnEighteenth-Century Italian Woman of Science by Gabriella Berti Logan for more information on Laura Bassi.
Margaret Eliza Maltby (1860-1944) was a recognized scientistand advocate for women in science. She overcame the education offered to women by taking extra courses in order to attend Oberlin College and receive a B.A. She studied with the Art Students’ League in New York City to explore her interest in art and then taught high school before enrolling as a “special student” at the Massachusetts Institute of Technology (MIT), receiving her B.S. Oberlin recognized this extra effort by awarding Dr. Maltby an M.S. She became a physics instructor at Wellesley College. She was encouraged in her graduate students by an AAUW fellowship to attend Göttingen University, which culminated in Dr. Maltby being the first American woman to receive a Ph.D. in physics from any German university. Dr. Maltby worked as an instructor, a researcher, and administrator in many universities and colleges in the U.S. and abroad. Her stature as a scientist was acknowledged with her entry in the first edition of AmericanMen of Science. She also was active in the AAUW, advocating for women to gain education and enter scientific fields. After her retirement from university life, she maintained her interest in the arts.

Frederic and Irene Joliot-Cure by By James Lebenthal
Irène Joliot-Curie (1897-1956) was a Nobel Prize Laureate for “artificial radioactivity.”  Born to  the woman every person thinks of as the epitome of a woman in science, Marie Curie, Irène had an extremely close relationship with her paternal grandfather. Her schooling was outside of the standard schooling type, her first years at home and her latter years in a science and math heavy co-operative school of Madame Curie’s colleagues. She received her Bachelor’s degree from the Collège Sévigné and went on to study at the Sorbonne. She received her doctorate in 1925 based on work with her mother at the Radium Institute of the Sorbonne. She married Frédéric Joliot, another research assistant of Madame Curie’s. Dr. Joliot-Curie continued her research, interrupted by a stint as Undersecretary of State for Scientific Research, one of the first high government posts to be offered to a woman. She worked as a professor for the Sorbonne and director of the Radium Institute, but was not admitted to the Academy of Sciences due to discrimination despite her work. She died, like her mother, of acute leukemia. Her scientific work was complemented by her love of physical activity and motherhood.
Katharine Burr Blodgett By Smithsonian Institution, U.S.
Katharine Burr Blodgett (1898-1979) was a woman with an amazing number of firsts.  Born to a widow, she was a world citizen in her formative years, attended high school at a private school in New York City, won a scholarship to attend Bryn Mawr, and graduated second in her class there. She received her Master’s degree from the University of Chicago, then headed off to work with Nobel Laureate Irving Langmuir at General Electric (GE) and becoming the first woman research scientist there. She was able to work with Nobel Laureate Sir Ernest Rutherford and earn her Ph.D. from Cambridge University as the first woman to earn a doctorate from Cambridge. She returned to GE. During her career, she invented many applications and is credited with six patents. She achieved much when many women did not, but her work was de-valued in the media. She did earn recognition from her peers, including the ACS Garvan Medal, the Photographic Society of America Progress Medal, and a day named after her in her hometown of Schenectady, NY. In addition to her scientific life, she enjoyed gardening, civic engagement, acting, and “dart[ing] about Lake George in a fast motor boat.”
Astrophysicist Charlotte Emma Moore Sitterly (1898-1990) was an authority on sun composition. She started her career as an excellent student with extracurricular interests, attending Swarthmore College to earn her B.A. Upon graduation, she accepted a position as a mathematics computer at Princeton University Observatory, one of the few employment opportunities available to science inclined women at the time. A stint at the Mount Wilson Observatory led to results published a 1928 monograph which was considered the authoritative work on the solar spectrum for four decades. She received her Ph.D. from the University of California, Berkeley in 1931. Her work earned her the Annie J. Cannon Prize, Silver and Gold Medals from the Department of Commerce, and several honorary doctorates in the U.S. and abroad. She was the first woman elected foreign associate by the Royal Astronomical Society of London. Her enthusiasm for her work continued until her death.

Maria Goeppert-Mayer By Nobel Foundation
Nuclear Physicist Maria Goeppert-Mayer (1906-1972)  was the second woman to win the  physics NobelHer early education was public education for girls followed by a private school founded by suffragettes. Circumstances led Dr. Goeppert-Mayer to take her exiting exams a year early, passing them she attended the University of Göttingen for her college education in mathematics. She continued to study physics at the University of Göttingen, earning her Ph.D. in 1930. She also married that year. The couple moved to America in hopes of better career trajectory for Dr. Goeppert-Mayer. Finding a position was difficult. When she had her first child, she stayed home with her for one year, then returned to research. While her positions were always part-time and not well recognized, she grew a well-respected network of collaborators. This network led to work with Hans Jensen which won her the Nobel Prize, shared with Jensen. Her network also eventually led to a full professorship position after 20 years of volunteer work. During this time, her health began to fail. She persevered with her work, publishing her last paper in 1965. The American Physical Society established an award in her honor in1985
Gertrude Scharff Goldhaber (1911-1998) was a respected researcher. She grew up in a time in Germany where girls were expected to become schoolteachers. She had a fascination with numbers, and eventually studied physics at the University of Munich, receiving her PhD in 1935. She fled Germany during the rise of the Nazis due to being Jewish, arriving in the United States and becoming a citizen in 1944. She had a wide involvement in the various National Laboratories studying nuclear physics. She also maintained several committee positions in the science community. She was also a strong advocate for women in the science community, forming a Women in Science group at Brookhaven National Lab and supporting other similar groups elsewhere. After her retirement from research, she continued interests in the history of science, outdoor activities, and art.
The Chicago Pile One Team 
Physicist, Molecular Spectroscopist Leona Woods MarshallLibby (1919-1986) Leona Woods grew up on a farm and was known for her inexhaustible energy. She attained her B.S. in chemistry from the University of Chicago when she was only 19 years old, and earned her PhD 5 years later. She worked as the only woman and youngest member of the Chicago Metallurgical Laboratory, a secret war group led by Enrico Fermi who built the world’s first nuclear fission reactor during her graduate work. Dr. Woods’ expertise was essential to the undertaking. She married another member of her team. She hid her first pregnancy until 2 days before her son’s birth. She took one week off before returning to work. Childcare was provided by her mother and sometimes Fermi’s bodyguard, John Baudino. Dr. Marshall was encouraged by Fermi as a female physicist. In the late 1950s, Dr. Marshall was divorced from her husband, pursuing her own career. In the early 1960s, Dr. Marshall moved to Colorado to work and married Willard Libby. Her mind was always considering any number of problems from many angles. She worked up until her death and was honored posthumously for her work, along with Lise Meitner, Marie Curie, and Irene Joliot-Curie.
Chien-Shiung Wu 
Chien-Shiung Wu (1912-1997) was a foremost experimental physicist of modern eraShe was encouraged as a girl to pursue her schooling as far as possible. This led her to teaching training, which lacked science so she taught herself physics, chemistry, and mathematics. She graduated high school with the highest grades in her class, earning her a place at the National Central University in Nanjing. She taught and did research upon graduation, then moved to the United States to pursue graduate studies. She earned her Ph.D. from the University of California – Berkeley in 1940, four years after leaving China. She was known for her expertise in nuclear fission and was consulted by top scientists. Despite this, her gender and nationality hindered her finding appropriate employment due to discrimination on both accounts. She married and started a teaching career, although she missed research. Upon the recommendation of Ernest Lawrence, she received offers from several Ivy League schools who were not accepting female students at the time. She became Princeton’s first woman instructor at that time. She was offered several positions, including back in China, but chose to remain in the U.S. to raise her son. She was unable to return to China until 1973. She worked at Columbia for many decades and earned accolades for her work.

Xide Xie (1921-2000) is a woman in China who needs no introductionHer early life involved much moving due to war and ill health, during which she taught herself English, calculus, and physics. She graduated in 1942 with a degree from Xiamen University. She moved to the United States to receive her master’s degree from Smith College in 1949 and her Ph.D. in physics from M.I.T. in 1951. She married in England and returned to China, despite the political climate. She taught and did research at the prestigious Fudan University. During the Cultural Revolution of 1966-76, she was detained, publicly humiliated, and endured breast cancer. After this upheaval, she returned to Fudan University, growing the physics department and achieving more esteemed positions in the University and government. She had also remained connected to her family, caring for her husband through lengthy illness. Her achievements were internationally recognized.

Awards Mentioned

Benedettini Academics were a select group of scholars from the Academy of Sciences created and named for Pope Benedict XIV to conduct research and present it annually at Academy meetings. This appointment escalated the prestige of the scientist above that given by being a member of the Academy of Sciences.

American Association for University Women (AAUW): Margaret Maltby received the European Fellowship from the Association of Collegiate Alumnae, which became the AAUW. This fellowship was specifically intended to help American women pursue graduate studies to circumvent rules that did not allow women to enroll in coeducational universities or earn graduate degrees.

The Nobel Prize is an international award given in several fields. It is one of the most prestigious awards for scientists in the eyes of the public.

The Garvan Medal is an award from the American Chemical Society to recognize distinguished service to chemistry by women chemists.
The Photographic Society of AmericaProgress Medal recognized a person who has made an outstanding contribution to the progress of photography or an allied subject. 
Annie Jump Cannon Prize is given to a North American female astronomer in the early stages of her career for her distinguished contribution to the field.
Department of Commerce Silver Medal, Gold Medal are the highest honors granted by the department for distinguished and exceptional performance.


Much of the information for this post came from the book Notable Women in the Physical Sciences: A Biographical Dictionary edited by Benjamin F. Shearer and Barbara S. Shearer.
Images for this post came from Wikimedia Commons

Adrienne M Roehrich, Double X Science Chemistry Editor


Modern Chemists

Our next installment of notable women in science brings us to chemists. Many of these women were born in the early part of the 20thcentury and forged their paths in tough times. All are still inspiring others today. Presented in no particular order:

Catherine Clarke Fenselau is a pioneer in mass spectrometryBorn in 1939, her interested in science was apparent before her 10th grade. She was encouraged to attend a women’s college, which at the time gave what she called “a special opportunity for serious-minded young women.” She graduated from Bryn Mawr with her A.B. in chemistry in 1961. Her graduate work at Stanford introduced her to the technology she would become known for, receiving her Ph.D. in analytical chemistry in 1965. Dr. Fenselau and her husband took positions at the Johns Hopkins University Medical School, at which time she had two sons. Johns Hopkins was under a mandate to accept female students and have female faculty at the time. Dr. Fenselau was made aware of the disparity of the treatment of male and female faculty, when in the 1970s the equal opportunity laws came into effect and she received an unexplained 25% raise. Her research resided in mass spectrometry, specifically in its use in biology. She became known as an anti-cancer researcher. Dr. Fenselau spoke often to chemists about feminism and goals, such as equal pay, opening closed career opportunities to women, and achieving the bonuses often only awarded to men. She has worked as an editor on several scientific journals. Some of her awards include the Garvan Medal, Maryland Chemist Award, and NIH Merit Award. Having  proper help at work and at home, and having supportive mentors and spouse has helped her achieve her success.

Elizabeth Amy Kreiser Weisburger is considered a real-lifemedical sleuth. Born in 1924, Dr. Weisburger was one of 10 children and schooled at home for her early education. She received her B.S. in chemistry, cum laude, Phi Alpha Epsilon from Lebanon Valley College. She received her Ph.D. in organic chemistry in 1947 from the University of Cincinnati. She married and had three children. Her research has caused her to be proclaimed a pioneer in the field of chemical carcinogenesis. She balanced her busy life of working at the NCI, committee work, giving lectures, attending meetings, writing and reviewing papers while caring for children with the aid of housekeepers and nursery childcare. Some of her awards include the Garvan Medal and the HillebrandPrize. Her life philosophy is summed up with “Don’t take life so seriously; you’ll never get out of it alive.”

Helen M. Free, photo from the ACS
Helen M. Free is a major contributor to science and science education. Born in 1923, Ms. Free attended the College of Wooster, graduating with honors and a B.S. in 1944. In 1978, she earned a M.A. from Central Michigan University. In the meantime, she worked as a chemist at Miles Laboratories. She developed clinical effective and easy to use laboratory tests. She worked her way up through the company and also held an adjunct professor position at Indiana University, South Bend. Ms. Free has used her time to be active in professional societies and has served as president for the American Association for Clinical Chemistry and the American Chemical Society. Her awards include the Garvan Medal, a Distinguished Alumni Award from Wooster, and is the first recipient ofthe Public Outreach Award bearing her name.

Jeanette Grasselli Brown is an industry researcher and director. Born in 1929, she graduated summa cum laudewith her B.S. from Ohio University in 1950 and received her M.S. in 1958 from Western Reserve University. She worked at Standard Oil of Ohio (now BP of America), and became the first woman director of corporate research there. She has received numerous awards including the Garvan Medal, Ohio Women’s Hall of Fame, and the Fisher Award in Analytical Chemistry. She has published 75 papers in scientific journals, written 9 books, and received 7 honorary Doctorate of Science degrees. She is an activist for the future of women in science.

Jean’ne Marie Shreeve is an important fluorine chemist. Born in 1933, she encountered sexism through her mother’s inability to be employed despite her training as a schoolteacher. Dr. Shreeve graduated with a B.A. from Montana State University in 1953, followed by an M.S. in 1956 from the University of Minnesota, and a Ph.D. in inorganic chemistry in 1961 from the University of Washington. After graduating, she worked her way through the professorial ranks at the University of Idaho. Besides her own research, Dr. Shreeve has devoted herself to educating other chemists. Some of her awards include U.S. Ramsey Fellow, Alfred P. Sloan Fellow, and Garvan Medal.

Joyce Jacobon Kaufman by Smithsonian Institution 
Joyce Jacobson Kaufman is distinguished in many fields. Born in 1929, she was reading before the age of 2 and was a voracious reader as a child. This led to her reading the biography of Marie Curie, which inspired her to be a chemist. Dr. Kaufman received her B.S., M.A., and Ph.D. in physical chemistry from Johns Hopkins University in 1949, 1959, and 1960, respectively. She married and had a daughter. Her research in the application of quantum mechanics to chemistry, biology, and medicine led to her renown in several fields. She has also spent much time in service positions. Her awards include the Martin Company Gold Medal for Outstanding Scientific Accomplishments (received 3 times), the Garvan Medal, and honored as one of ten Outstanding Women in the State of Maryland.

Madeleine M. Joullie is known for elegant research and inspirational teachingBorn in 1927, her early life in Brazil was overly-protective, so her father encouraged her to attend school in the U.S.A. She received her B.Sc. from Simmons College in 1949, and her M.Sc. and Ph.D. in chemistry in 1950 and 1953, respectively, from the University of Pennsylvania. She then worked her way through the professorial ranks at the University of Pennsylvania. Initially, only the women graduate students would work with her, and they were few and far between. She has explored many research avenues over the course of her career. Her awards include the Garvan Medal, the American Cyanamid Faculty Award, the Henry HillAward, and the Lindback Award for Distinguished Teaching.

Marjorie Caserio is a researcher, educator, author, andacademic administrator. Born in 1929, she entered university with the goal of becoming a podiatrist in order to generic income. She received several rejections from colleges due to her gender, and eventually was accepted to be the only woman in her class. She received her B.S. from Chelsea College, University of London in 1950 and an M.A. and Ph.D from Bryn Mawr in 1951 and 1956. Dr. Caserio is co-author of one of the most popular organic chemistry textbooks in the chemistry during the 1960s and 1970s. Her awards include the Garvan Medal and John S. Guggenheim Foundation Fellow.

Mary Lowe Good has won several awards and is a public servant. Born in 1931, she was supported in her aspirations by her parents. She received her B.S. in 1950 from the University of Central Arkansas, which was then the Arkansas State Teachers College. She went on to receive her M.S. and Ph.D. in inorganic and radiochemistry from the University of Arkansas in 1953 and 1955. Her career began in academic, but an appointment to the National Science Foundation by President Carter changed the course of her career. She served the International Union of Pure and Applied Chemistry, and president of the American Chemical Society and Zonta International Foundation. Some of her awards include Garvan Medal, CharlesLathrop Parsons Award, and 18 honorary doctorates.

Ruth Mary Roan Benerito is an academic and government scientistBorn in 1916, she began college at the age of 15 at Sophie Newcomb College, the women’s college of Tulane and received her B.S. in 1935. She received her M.S. from Tulane University in 1938, which she worked half-time while working another job at the same time. She taught at Tulane and its colleges before going to the University of Chicago to get her Ph.D. in 1948 in physical chemistry, again working on a part-time basis. Her career oscillated between academia and industry, earning her a large number of awards, including the Federal Women’s Award, the Southern Chemist Award, and inducted as a Fellow into the American Institute of Chemists and Iota Sigma Pi.  

Awards

The Garvan Medal is an award from the American Chemical Society to recognize distinguished service to chemistry by women chemists.

The Maryland Chemist Award recognizes and honors its members for outstanding achievement in the fields of chemistry.

The NIH Merit Award is a symbol of scientific achievement in the research community.

The Hillebrand Prize is awarded for original contributions to the science of chemistry.

The Distinguished Alumni Award from Wooster is presented annually to alumni who have distinguished themselves in one of more of the following area: professional career; service to humanity; and service to Wooster.

Helen M. Free Award recognizes outstanding achievements in the field of public outreach. 

Ohio Women’s Hall of Fame provides public recognition of contributions made to the growth and progress of Ohio and the nation.
The Fisher Award in Analytical Chemistry recognizes outstanding contributions to the field of analytical chemistry.

U.S. Ramsey Fellow is no longer offered.

Alfred P. Sloan Fellow is awarded to scientists and scholars of outstanding promise.

Outstanding Women in the State of Maryland awards women under the age of 40 for their achievements already made in an early career. 

The American Cyanamid Faculty Award  

The Henry Hill Award recognizes distinguished service to professionalism. 


John S. Guggenheim Foundation Fellow is awarded for demonstrating outstanding scholarship.

Charles Lathrop Parsons Award recognizes outstanding public service. 



The American Institute of Chemists advances the chemical sciences by establishing high professional standards of practice and to emphasize the professional, ethical, economic, and social status of its members for the benefit of society as a whole.

Iota Sigma Pi is a national honor society for women in chemistry.

Much of the information for this post came from the book Notable Women in the Physical Sciences: A Biographical Dictionary edited by Benjamin F. Shearer and Barbara S. Shearer. 

Adrienne M Roehrich, Double X Science Chemistry Editor

Diversity in Science Carnival #14: Women’s History Month–Exploring the role of women in the STEM enterprise

Women in Science, via the Smithsonian.

“We must believe that we are gifted for something.” Marie Curie

Image of a real Rosie the Riveter from the
Women’s History Month site.
It’s tempting to cast the role of women in STEM (Science, Technology, Engineering, and Math) as one of struggles and battles because of their sex, rather than as one of contributions because of their minds. But for Women’s History Month and this Diversity in Science Carnival #14, our focus is the role of women in the enterprise of STEM. There’s more to a woman than her sex and her struggles in science–there is, after all, the enormous body of work women have contributed to science.

 

Our history is ongoing, but we can start with a look back. Thanks to the efforts of the Smithsonian Institution Archives, we can put faces to the names of some of the female STEMmers of history. In a presentation of photographs in an 8 by 9 space, we can see the images of 72 women who contributed to the enterprise of STEM, many of them involved with the Smithsonian in some capacity. As their clothes and the dates on the photos tell us, these women were doing their work in a time when most women didn’t even wear pants.  
Some are Big Names–you’ve probably heard of Marie Curie. But others are like many of us, women working in the trenches of science, contributing to the enterprise of STEM in ways big and small. Women like Arlene Frances Fung, whose bio tells us she was born in Trinidad, went to medical school in Ireland, and by 1968 was engaged in chromosome research at a cancer institute in Philadelphia. From Trinidad to cancer research, her story is one of the millions we could tell about women’s historical contributions to science, if only we could find them all. But here there are 72, and we encourage you to click on each image, look at their direct gazes, ponder how their interest in science and knowledge trumped the heavy pressures of social mores, and discover the contributions these 72 women made, each on her own “little two inches wide of ivory.”

For more on historical and current women in science, you can also see Double X Science’s “Notable Women in Science” series, curated by Adrienne Roehrich.

And then there are the women STEMmers of today, who likely are, according to blogger Emma Leedham writing at her blog Pipettes and Paintbrushes, still underpaid. Leedham also mulls here what constitutes a role model for women–does it require being both a woman and a scientist, or one or the other?

Laurel L. James
Laurel L. James, writing at the University of Washington blog for the school’s SACNAS student chapter, answers with her post, “To identify my role as a woman in science: I must first honor my mother, my family and my past.” Her mother was the first “Miss Indian America,” and Laurel is a self-described non-traditional student at the school, where she is a graduate student in forest resources. She traces her journey to science, one that involved role models who were not scientists but who, as she writes, showed her “how to hang onto the things that are important with the expectation of getting something in return all the while, persevering and knowing who you are; while walking with grace and dignity.” I’d hazard that these words describe many a woman who has moved against the currents of her society to contribute something to the sciences.

A great site, Steminist.com, which features the “voices of women in science, tech, engineering, and math,” runs a series of interviews with modern-day STEMmers, including Double X Science’s own Jeanne Garbarino, and Naadiya Moosajee, an engineer and cofounder of South African Women in Engineering. You can follow Naadiya on Twitter here. Steminist is also running their version of March Madness, except that in honor of Women’s History Month, we can choose “Which historical women in STEM rock (our) world.” The 64 historical STEMinists in the tourney are listed here and include Emily Warren Robling (left), who took over completion of the Brooklyn Bridge when her husband’s health prevented his doing so; she is known as the first woman field engineer. Double X Science also has a series about today’s women in science, Double Xpression, which you can find here.

Today, you can find a woman–or many women–in STEM just about anywhere you look, whether it is as a government scientist at NOAA like Melanie Harrison, PhD, or at NASA. It hasn’t always been that way, and it can still be better. But women have always been a presence in STEM. In the 18thand 19th centuries, astronomer Caroline Herschellabored away through the dark hours of just about every night of her adult life, tracking the night sky. Today, women continue these labors, and STEM wouldn’t be what it is today without women like Herschel willing to stay up all night with the skies or spend days on end in the field or lean over a microscope for hours just to add a tiny bit more to what we know about our world and our universe.

                            

Caroline Herschel
For women in science, we’re there–at night, in the lab, in the field–because we love science. But as the non-science role models seem to tell us, we stick to it–and can stick with it–because we had role models in and out of science who showed us that regardless of our goals, our attitudes and willingness to move forward in spite of obstacles are really what drive us to success in STEM careers. Among the links I received for this carnival was one to Science Club for Girls, which is sponsoring a “Letter to My Young Self” roundup for Women’s History Month. The letters I’ve read invariably have that “stick with it” message, but one stood out for me, and I close with a quote from it.

It’s a letter by Chitra Thakur-Mahadik, who earned her PhD in biochemistry and hemoglobinopathy from the University of Mumbai and served as staff scientist a Mumbai children’s hospital for 25 years. She wrote to her younger, “partially sighted” self that, “The future is ahead and it is not bad!” She goes on to say, “Be fearless but be compassionate to yourself and others… be brave, keep your eyes and ears open and face the world happily. What if there are limitations? Work through them with awareness. –Yours, Chitra”
Links and resources for women in STEM, courtesy of D.N. Lee

Stay tuned for the April Diversity in Science Carnival #15: Confronting the Imposter Syndrome. This topic promises to resonate for many groups in science. I’m pretty sure we’ve all felt at least of twinge of imposter syndrome at some point in our education and careers.  Your editor for this carnival will be the inimitable Scicurious, who  blogs at Scientific American and Scientopia.




UPDATE: Carnival #15 is now available! Go read about imposter syndrome, why it happens, who has it, and what you can do about it. 

By Emily Willingham, DXS managing editor