Freezing Point: Science never tasted so good!

Learning about freezing point can lead to a tasty reward!

When trying to devise cool activities for my kids, I generally stick with either a culinary or a scientific theme.  This is mostly because cooking and science are what I know best.  But when the opportunity arises to combine the two in a fun-filled, hands-on, and awesomely secret educational activity, I do my best to keep from micturating in my undergarments. 

In my experience, the best example of culinary science fusion involves a lesson on the concept of freezing point, mainly because the end product of this stealth lesson can be topped with whipped cream and a cherry.  That’s right, I’m talking about teaching science while making ice cream.

To fully appreciate the culinary chemistry behind this frozen delight, it’s important to understand the concept of freezing point and melting point.  Simply put, the freezing point is the temperature at which a liquid freezes and the melting point is the temperature at which a solid melts.  For most substances, the melting point and the freezing point are the same. 

Let’s use water as an example.  If water is cooled below 0°C (32°F), it will transform into ice.  Therefore, the freezing point of water is 0°C.  However, if the temperature of ice is raised above 0°C, it will melt.  Therefore, the melting point of water is also 0°C. 

HOWEVER, these points can be manipulated.  For anyone who lives in an area where winter happens, you’ve probably seen the massive seasonal salt inventory at The Home Depot.  The idea is that by putting salt on walkways, usually in the form of either rock salt (NaCl) or calcium chloride (CaCl2), you will prevent the build up of ice and snow and thus prevent any nasty slips.  This is because salt will lower the freezing point of water, thereby helping to keep it from turning into an icy mess, even when temperatures are below freezing.  But, it will only work if the walkway is warmer than -9°C (or 15°F). 

How does this relate back to ice cream?  Well, we can use the same idea of lowering the freezing point of water and apply it to making cream freeze.  The set-up involves two resealable plastic bags (one quart-sized and one gallon-sized), ice, lots of salt, cream, milk, sugar, vanilla, and your flavoring of choice. 

Into the quart-sized resealable plastic bag, combine the cream, milk, sugar, vanilla, and flavoring (follow the recipe below and ensure that the bag is fully sealed).  Fill the second resealable plastic bag about halfway with crushed ice and all of the salt.  Place the cream-filled bag into the ice-filled bag and seal.  Then…shake! 

When salt is added to the ice water, the temperature of the mixture drops.  Because the temperature of the ice-salt mixture is lower than the cream mixture, a temperature gradient is created and the cream mixture easily freezes.  After about five to ten minutes of shaking, you will have yourself some fresh-churned sciencey deliciousness!  Enjoy!


Science Experiment Ice Cream:

½ Cup Heavy Cream

½ Cup Milk

¼ Cup Sugar

¼ Tsp. Real Vanilla Extract

Crushed or Shaved Ice

1 Cup of Table Salt or Sea Salt

1 Quart-Sized Ziploc Bag

1 Gallon-Sized Ziploc Bag

Here is a video of my and a few of my pals doing this experiment with my daughter.  We did this last year and my daughter STILL talks about it!  



The set-up:

Shakin’ it up:

The big reveal: 


For more information check these out:

General Chemistry Online Why does salt melt ice?


Jeanne Garbarino, Double X Science Editor

Why Are Snowflakes Always Six-Sided?

(Today’s offering is a guest post by engineer Linda Gaines.)

It’s a well-known fact that all snowflakes have six sides. Or at least I thought it was. Why Google is unable to Google that fact and has on at least two occasions created a Doodle with an eight-sided snowflake is a mystery. What’s less mysterious is how scientists can be so sure that all snowflakes have six sides. Have we examined all snowflakes? No, of course not, but the explanation lies in two words: hydrogen bonding. Thanks to the intermolecular force of hydrogen bonding, all snowflakes have six sides, and hydrogen bonding also makes life as we know it possible. Now that’s an important bond.

You can’t really understand hydrogen bonding, though, without understanding why water molecules are arranged like they are. Water seems like a simple enough molecule. It consists of one oxygen atom with two hydrogen atoms bonded to it. The hydrogen atoms bond to the oxygen atom at a distance of exactly 104.5 degrees from each other (1). Why that particular angle?

An oxygen atom has a total of eight electrons. Two of them take up all the available spots in the shell closest to the atom’s nucleus. The remaining six electrons are relegated to the atom’s outermost (or valence) electronic shell. But this shell can actually hold eight electrons, so two spots are open. A hydrogen atom has one electron on its only electronic shell, and since that shell holds two electrons, it’s got room for one more.

Because oxygen has two available spaces and hydrogen has one, oxygen can share that space with two hydrogen atoms. Both hydrogen atoms share their single electron with the oxygen, and the oxygen shares an electrons with each of the hydrogen atoms. The remaining four of the oxygen’s electrons aren’t a part of this sharing arrangement, though. Electrons kick around in pairs, so these four non-sharing electrons form two pairs.

With these two pairs sitting alone and the other two electrons each sharing with a hydrogen, a water molecule has a tetrahedron (or three-sided pyramid) shape with four attachments emerging from the oxygen nucleus. Two of those attachments are electron clouds containing two electrons each (the pairs), and the other two attachments are hydrogen atoms with two electrons moving between the oxygen and hydrogen orbits. In a true tetrahedron, the attachments would all be 109.5 degrees from each other. With the water molecule, though, the hydrogen atoms are 104.5 degrees from each other because the two paired-electron clouds are grabby with space and force the electrons shared with the hydrogen atoms a little closer together.

So we’ve learned that the hydrogen and oxygen form a covalent bond, which means they share their electrons. What I haven’t told you is that the oxygen is very grabby with that electron, so the sharing isn’t exactly equal. The oxygen has a stronger hold on the electron and is pulling that negative charge closer to it and away from the hydrogens. What results is a slightly negative oxygen and slightly positive hydrogens. The oxygen actually has two areas of negativity, right across from where it’s bonded with each hydrogen. Water molecules can use these areas of slight charge to form a fairly strong bond with other molecules, a bond called a hydrogen bond. While not every molecule containing hydrogen can form this kind of bond with other molecules, molecules in which hydrogen is in this unequal sharing situation will be able to.

In the case of water molecules bonding to other water molecules, the two slightly negative areas of the oxygen can each bond with a slightly positive hydrogen from another water molecule. When all four slightly charged areas have each bonded with another water molecule via hydrogen bonding, the result is a tetrahedral (four-sided pyramid) shape.

These bonds make water an unusual substance. When the temperature drops and water starts to solidify, the hydrogen bonding becomes very important. The hydrogen bonding dictates the shape of the ice crystals. You’ve learned that each water molecule is linked to four other water molecules in a tetrahedral arrangement. 

As the water freezes, these tetrahedrons come closer together and crystallize into a six-ring or hexagonal structure. Look at the image to see how this happens. Each point on the hexagon is an oxygen atom, and each side is a hydrogen bonded to one oxygen. As the water approaches freezing temperature, the water molecules continue to crystallize in this tetrahedral arrangement.

But water does something unlike most substances. As it nears freezing, instead of continuing to contract, it expands slightly from about 4 degrees to 0 degrees Celsius as the motion of the molecules slows with the cold, and the hydrogen bonds extend the molecules to their fullest distance from each other. It’s like a ring of people holding hands, elbows bent, and then gradually straightening their arms to the fullest extension so that they’re at the greatest distance from each other. When water molecules do this, the hexagonal structure expands into a larger and larger hexagonal structure.

The snowflake, with its six sides, is what results from this process: It is a large, gorgeous ice crystal. Ice crystals are like mineral rock crystals. The macroscopic (large) shape you see is dictated by the microscopic, molecular crystalline structure. Ice has a hexagonal crystalline structure, so a snowflake has a hexagonal structure. Sodium chloride, aka table salt, has a cubic molecular structure, so the salt crystals you shake on your food have a cubic shape.

It’s interesting that hydrogen bonding causes snowflakes to be six sided (are you listening, Google?), but it carries far greater consequences than beautiful snowflakes. Breaking those hydrogen bonds apart so that water can transform from liquid to gas takes a lot of heat, so the boiling point of water is much higher than it is for other, similar molecules. Based on similar molecules, water’s boiling point should be about -80 degrees Celsius (-176 degrees Fahrenheit) (!) instead of the 100 degrees Celsius (212 degrees Fahrenheit) it really is (1).

And then there’s the fact that ice floats, which means that the solid form of water is less dense than the liquid form. It is highly unusual for the solid form of a substance to be less dense than its liquid. But because those hydrogen bonds force water into a pretty open, hexagonal crystalline structure as the temperature nears 0 degrees Celsius, molecules are not packed as closely together as they are at warmer temperatures.


Think of those people holding hands, stiff-arming each other as far apart as possible. If they all started slam dancing, their handholds would break, and they could get closer to one another. Water molecules are a bit like that when the temperature goes above 4 degrees Celsius. When ice melts, some of the hydrogen bonds break, and the water molecules can be closer together. The far-apart water molecules in ice form a less-dense substance than the close-together molecules of liquid water, so ice floats in liquid water.

This property of water is integral to life on Earth. When a freshwater lake starts to freeze, the ice floats on the top, insulating the water below and preventing it from freezing. The fish, plants, and other life in the lake remain alive beneath the protective and insulating icy layer. If ice sank instead, over periods of deep freeze during its 4.5 billion year existence, this blue planet would have developed an icy, inhospitable core. Instead, the fact that ice floats meant that Earth was a perfect incubator for life in its oceans. All because oxygen is just a little bit grabby with electrons.

(1) Petrucci, Ralph H. (1989) General Chemistry (Fifth Edition). New York: MacMillan.

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

Why blueberries won’t turn you blue and other blueberry facts

Blueberries. Credit.


by Adrienne Roehrich, Chemistry Editor

Blueberries in the Northwestern semisphere are the fruit of several shrubs in the genus Vaccinium L.  They grow in all provinces in Canada and all but two of the United States (Nebraska and North Dakota). In the Northwestern semisphere, one can find 43 species of blueberries, depending on the region. Blueberries are found and produced in all hemispheres of the world. However, the species can vary by region.

Taxonomy:
Kingdom: Plantae (Plants)
Subkingdom: Tracheobionta (Vascular plants)
Subdivision: Spermatophyta (Seed plants)
Division: Magnoliophyta (Flowering plants)
Class: Magnoliopsida (Dictyledons)
Subclass: Dilleniidae
Order: Ericales
Family: Ericaceae
Genus: Vaccinium

There are 43 species and 46 accepted taxa overall. Some of the species include fruits we do not necessarily recognize as blueberry, including farkleberry, bilberry, ohelo, cranberry, huckleberry, whortleberry, deer berry, and lingonberry.  (Source

Blueberries are a very popular fruit in the U.S., and is consumed in fresh, frozen, and canned forms. While blueberries are a great fruit to eat to meet your suggested fruit intake, it also is one of the foods that are purported to have properties that it just does not have. This undeserved reputation results from the high levels of anti-oxidants, leading those predisposed to looking for “super foods” to classify blueberries into the anti-oxidant super food category. While eating more healthy foods is always a good idea, no food has curative effects all on its own.

Other aspects of blueberry nutrition includes it as a source of sugar. One cup (148 g) of blueberries contains about 15 g of sugar and 4 g of fiber, a single gram of protein, and half a gram of fat. If you are counting carbs, this cup has 21 g of them. That one cup of blueberries averages about 85 calories, which is approximately the same as a medium apple or orange. While almost all the vitamins and minerals nutrition gurus like to report on are present to some amount, for the 2000-calorie diet, that one cup of blueberries will provide the recommended daily value of 24% of Vitamin C, 36% of Vitamin K, and 25% of manganese. The remaining values range from 0-4%. (Values obtained from Nutrition.com and verified through multiple sources.)

The Wikipedia entry is quite good and well researched (as of August 18, 2012). 

The photo above shows all of the life stages of a blueberry. Berries go from the little red nub at the end of the branch to round and juicy blueberries through fertilization of the ovary, which swells rapidly for about a month, then its growth ceases. The green berry develops with no change in size. The chemicals responsible for the blue color, anthocyanins, begin to turn the berry from green to blue as it develops over about 6 days. The volume of the berry increases during the change in color phase.

Will blueberries turn you blue? In short, no. You can achieve blue skin through the ill-advised practice of drinking silver or you can achieve orangish-yellow skin by eating a large number of carrots. This is because the chemicals causing the skin color are fat soluble and are present in a large quantity in the fat just under the skin, giving the skin those colors. Anthocyanin, the primary chemical causing the blue color in blueberries, is not fat soluble and will not reside in the fat under your skin.

Anthocyanins is a class of over 30 compounds. The chemical structure is generally as shown below. They are polyphenolic, which indicates the 3 ring structures. The “R” indicates different functional groups that change depending on which anthocyanin the structure represents. 


Interestingly, anthocyanins are also pH indicators because their color ranges from yellow to red to blue depending on the local pH. The blue color indicates a neutral pH. The wikipedia page on anthocyanins is also informative (as of August 18, 2012). 

As mentioned before, blueberries are a popular fruit. Recipes abound, but here is one from my own Recipe Codex for Surprise Muffins with blueberries:

Ingredients
  • 6 Tbsp. butter
  • 3/4 cup sugar
  • 2 eggs
  • 1/2 cup milk
  • 1/2 – 1 pint blueberries, fresh or frozen (defrosted)
  • Food coloring, optional
  • 2 cups all-purpose flour
  • 1/4 tsp. salt
  • 1 Tbsp. baking powder
  • Your favorite mini-treat (Hershey’s Kisses, Hugs, Reese’s Mini Cups, strawberry jam, etc.)
Directions
  1. Preheat the oven to 350º. In a large bowl, cream the butter and sugar. You can use a wooden spoon, a potato masher or handheld electric mixer. Mix in the eggs, one at a time, and add the milk.
  2. Rinse the strawberries and cut off the green stem. Mash the berries with a potato masher or puree in a blender. Then stir the berries into the butter and milk mixture. TIP: For muffins with a more blue color, add a few drops of blue food coloring.
  3. In a separate bowl, sift the flour, salt and baking powder. Stir well. Add the flour mixture to the berry mixture. Use a wooden spoon to stir until all the white disappears.
  4. Line the muffin tin with paper liners. Drop the batter from a tablespoon to fill the cups halfway.
  5. Add a surprise: an unwrapped mini treat or 1/2 teaspoon of jam. Then spoon more batter to fill almost to the top.
  6. Bake until the muffins begin to brown and a toothpick inserted near the center (but not in the mini-treat) comes out clean, about 20-25 minutes.
  7. Remove the muffins from the tin and cool.
Or perhaps you are in less of a cooking scientist mood and more in a home lab mood. Try this at-home lab with blueberries about dyes. Adapted from the Journal of Chemical Education.

Items You Need
  • 4 microwavable/stove top staff glasses, pots, or containers at least 1/2 cup in volume
  • tablespoons or 1/4 cup measuring cup
  • water
  • spatula
  • alum (available in the grocery store spice aisle)
  • cream of tartar (available in the grocery store spice aisle)
  • hot pads and tongs
  • at least four small (1-2 in.) squares of white cotton cloth
  • yellow onion skins
  • blueberries
  • spoon
  • paper towels
  • vinegar
  • baking soda
  • a dropper
  • notebook for experimental observations
Procedure
In each step, you will want to record your observations, paying special attention to colors.
  1. Pour 4 tablespoons (1/4 cup) into container 1. Add a pea-sized scoop of alum and about half that amount of cream of tartar and stir. Bring the solution to a boil on the stove top or by microwaving for about 60 seconds. (Your microwave may vary.) Add two small squares of white cotton cloth and boil for two minutes. Set the container aside. The squares will be used in steps 4 and 6.
  2. Tear the outer, papery skin from a yellow onion into pieces no more than 1 inch square. Place enough pieces in a second container to cover its bottom with  2 or 3 layers of onion skin. Add about 4 tablespoons of water to the container. Bring the solution to a boil on the stove top, continuing to boil for 5  minutes.
  3. Wet a new square of cloth with water. Place it in container 2 so it is completely submerged and boil for 1 minute. Using tongs, remove the cloth and rinse it with water. Place the cloth square in the appropriate area on a labeled paper towel.
  4. Use tongs to remove one of the cloth squares from beaker 1. Repeat step 3 using this square. Compare to the dyed cloth square from step 3.
  5. Pour 4 tablespoons of water in a third container. Add 4-5 blueberries to the container and mash them with a spoon. Bring the solution to a boil on the stove, and continue to boil for 5 minutes.
  6. Repeat steps 3 and 4 substituting the blueberry mixture in container 3 for the onion skin mixture in container 2.
  7. Mix a small scoop of baking soda with a tsp of water in a clean container. With a dropper, place 1-2 drops of the baking soda solution in one corner of each cloth square. What happens? Rinse the dropper thoroughly, then place 1-2 drops of vinegar on the opposite corner of each square. What happens? Rinse the fabric squares under cool running water. Is there a change? Allow the squares to dry overnight. Is there any change of the cloth dries?
Optional: Try variations in the procedure such as changing the amount of dye source, the length of time the cloth spends in the dye solution, and the temperature of the dye solution.

Questions to consider
The solution in step 1 is called a mordant. Based on your observations, what is the purpose of a mordant?
Is the dye produced by blueberries really blue? Why might some people not want to wear clothes dyed with blueberries?

———————-
All in all, enjoy your blueberries. As a shrub, it is quite pretty. As a fruit, it is quite yummy. And as the tool in an experiment, it is quite fun.

These views are the opinion of the author and do not necessarily reflect or disagree with those of the DXS editorial team.

Science, health, medical news freaking you out? Do the Double X Double-Take first

Handy short-form version.

Have you seen the headlines? Skip them
You’ve probably seen a lot of headlines lately about autism and various behaviors, ways of being, or “toxins” that, the headlines tell you, are “linked” to it. Maybe you’re considering having a child and are mentally tallying up the various risk factors you have as a parent. Perhaps you have a child with autism and are now looking back, loaded with guilt that you ate high-fructose corn syrup or were overweight or too old or too near a freeway or not something enough that led to your child’s autism. Maybe you’re an autistic adult who’s getting a little tired of reading in these stories about how you don’t exist or how using these “risk factors” might help the world reduce the number of people who are like you.

Here’s the bottom line: No one knows precisely what causes the extremely diverse developmental difference we call autism. Research from around the world suggests a strong genetic component [PDF]. What headlines in the United States call an “epidemic” is, in all likelihood, largely attributable to expanded diagnostic inclusion, better identification, and, ironically, greater awareness of autism. In countries that have been able to assess overall population prevalence, such as the UK, rates seem to have held steady at about 1% for decades, which is about the current levels now identified among 8-year-olds in the United States. 

What anyone needs when it comes to headlines honking about a “link” to a specific condition is a mental checklist of what the article–and whatever research underlies it–is really saying. Previously, we brought you Real vs Fake Science: How to tell them apart. Now we bring you our Double X Double-Take checklist. Use it when you read any story about scientific research and human health, medicine, biology, or genetics.

The Double X Double-Take: What to do when reading science in the news
1. Skip the headline. Headlines are often misleading, at best, and can be wildly inaccurate. Forget about the headline. Pretend you never even saw the headline.

2. What is the basis of the article? Science news originates from several places. Often it’s a scientific paper. These papers come in several varieties. The ones that report a real study–lots of people or mice or flies, lots of data, lots of analysis, a hypothesis tested, statistics done–is considered “original research.” Those papers are the only ones that are genuinely original scientific studies. Words to watch for–terms that suggest no original research at all–are “review,” “editorial,” “perspective,” “commentary,” “case study” (these typically involve one or only a handful of cases, so no statistical analysis), and “meta-analysis.” None of these represents original findings from a scientific study. All but the last two are opinion. Also watch for “scientific meeting” and “conference.” That means that this information was presented without peer review at a scientific meeting. It hasn’t been vetted in any way.

3. Look at the words in the article. If what you’re reading contains words like “link,” “association,” “correlation,” or “risk,” then what the article is describing is a mathematical association between one thing (e.g., autism) and another (e.g., eating ice cream). It is likely not describing a biological connection between the two. In fact, popular articles seem to very rarely even cover scientific research that homes in on the biological connections. Why? Because these findings usually come in little bits and pieces that over time–often quite a bit of time–build into a larger picture showing a biological pathway by which Variable 1 leads to Outcome A. That’s not generally a process that’s particularly newsworthy, and the pathways can be both too specific and extremely confusing.

4. Look at the original source of the information. Google is your friend. Is the original source a scientific journal? At the very least, especially for original research, the abstract will be freely available. A news story based on a journal paper should provide a link to that abstract, but many, many news outlets do not do this–a huge disservice to the interested, engaged reader. At any rate, the article probably includes the name of a paper author and the journal of publication, and a quick Google search on both terms along with the subject (e.g., autism) will often find you the paper. If all you find is a news release about the paper–at outlets like ScienceDaily or PhysOrg–you are reading marketing materials. Period. And if there is no mention of publication in a journal, be very, very cautious in your interpretation of what’s being reported.

5. Remember that every single person involved in what you’re reading has a dog in the hunt. The news outlet wants clicks. For that reason, the reporter needs clicks. The researchers probably want attention to their research. The institutions where the researchers do their research want attention, prestige, and money. A Website may be trying to scare you into buying what they’re selling. Some people are not above using “sexy” science topics to achieve all of the above. Caveat lector

6. Ask a scientist. Twitter abounds with scientists and sciencey types who may be able to evaluate an article for you. I receive daily requests via email, Facebook, and Twitter for exactly that assistance, and I’m glad to provide it. Seriously, ask a scientist. You’ll find it hard to get us to shut up. We do science because we really, really like it. It sure ain’t for the money. [Edited to add: But see also an important caveat and an important suggestion from Maggie Koerth-Baker over at Boing Boing and, as David Bradley has noted over at ScienceBase, always remember #5 on this list when applying #6.] 

—————————————————————————–

Case Study
Lately, everyone seems to be using “autism” as a way to draw eyeballs to their work. Below, I’m giving my own case study of exactly that phenomenon as an example of how to apply this checklist.

1. Headline: “Ten chemicals most likely to cause autism and learning disabilities” and “Could autism be caused by one of these 10 chemicals?” Double X Double-Take 1: Skip the headline. Check. Especially advisable as there is not one iota of information about “cause” involved here.

2. What is the basis of the articleEditorialConference. In other words, those 10 chemicals aren’t something researchers identified in careful studies as having a link to autism but instead are a list of suspects the editorial writers derived, a list that they’d developed two years ago at the mentioned conference. 

3. Look at the words in the articles. Suspected. Suggesting a link. In other words, what you’re reading below those headlines does not involve studies linking anything to autism. Instead, it’s based on an editorial listing 10 compounds [PDF] that the editorial authors suspect might have something to do with autism (NB: Both linked stories completely gloss over the fact that most experts attribute the rise in autism diagnoses to changing and expanded diagnostic criteria, a shift in diagnosis from other categories to autism, and greater recognition and awareness–i.e., not to genetic changes or environmental factors. The editorial does the same). The authors do not provide citations for studies that link each chemical cited to autism itself, and the editorial itself is not focused on autism, per se, but on “neurodevelopmental” derailments in general.

4. Look at the original source of information. The source of the articles is an editorial, as noted. But one of these articles also provides a link to an actual research paper. The paper doesn’t even address any of the “top 10″ chemicals listed but instead is about cigarette smoking. News stories about this study describe it as linking smoking during pregnancy and autism. Yet the study abstract states that they did not identify a link, saying “We found a null association between maternal smoking and pregnancy in ASDs and the possibility of an association with a higher-functioning ASD subgroup was suggested.” In other words: No link between smoking and autism. But the headlines and how the articles are written would lead you to believe otherwise. 

5. Remember that every single person involved has a dog in this hunt. Read with a critical eye. Ask yourself, what are people saying vs what real support exists for their assertions? Who stands to gain and in what way from having this information publicized? Think about the current culture–does the article or the research drag in “hot” topics (autism, obesity, fats, high-fructose corn syrup, “toxins,” Kim Kardashian) without any real basis for doing so? 

6. Ask a scientist. Why, yes, I am a scientist, so I’ll respond. My field of research for 10 years happens to have been endocrine-disrupting compounds. I’ve seen literally one drop of a compound dissolved in a trillion drops of solvent shift development of a turtle from male to female. I’ve seen the negative embryonic effects of pesticides and an over-the-counter antihistamine on penile development in mice. I know well the literature that runs to the thousands of pages indicating that we’ve got a lot of chemicals around us and in us that can have profound influences during sensitive periods of development, depending on timing, dose, species, and what other compounds may be involved. Endocrine disruptors or “toxins” are a complex group with complex interactions and effects and can’t be treated as a monolith any more than autism should be.

What I also know is that synthetic endocrine-disruptors have been around for more than a century and that natural ones for far, far longer. Do I think that the “top 10″ chemicals require closer investigation and regulation? Yes. But not because I think they’re causative in some autism “epidemic.” We’ve got sufficiently compelling evidence of their harm already without trying to use “autism” as a marketing tool to draw attention to them. Just as a couple of examples: If coal-burning pollution (i.e., mercury) were causative in autism, I’d expect some evidence of high rates in, say, Victorian London, where the average household burned 11 tons of coal a year. If modern lead exposures were causative, I’d be expecting records from notoriously lead-burdened ancient Rome containing descriptions of the autism epidemic that surely took it over. 

Bottom line: We’ve got plenty of reasons for concern about the developmental effects of the compounds on this list. But we’ve got very limited reasons to make autism a focal point for testing them. Using the Double X Double-Take checklist helps demonstrate that.

By Emily Willingham, DXS managing editor 

Real science vs. fake science: How can you tell them apart?


Phrenology is a famous pseudoscience that involved determining
a person’s personality based on bumps on the skull.

Pseudoscience is the shaky foundation of practices–often medically related–that lack a basis in evidence. It’s “fake” science dressed up, sometimes quite carefully, to look like the real thing. If you’re alive, you’ve encountered it, whether it was the guy at the mall trying to sell you Power Balance bracelets, the shampoo commercial promising you that “amino acids” will make your hair shiny, or the peddlers of “natural remedies” or fad diet plans, who in a classic expansion of a basic tenet of advertising, make you think you have a problem so they can sell you something to solve it. 

Pseudosciences are usually pretty easily identified by their emphasis on confirmation over refutation, on physically impossible claims, and on terms charged with emotion or false “sciencey-ness,” which is kind of like “truthiness” minus Stephen Colbert. Sometimes, what peddlers of pseudoscience say may have a kernel of real truth that makes it seem plausible. But even that kernel is typically at most a half truth, and often, it’s that other half they’re leaving out that makes what they’re selling pointless and ineffectual.

If we could hand out cheat sheets for people of sound mind to use when considering a product, book, therapy, or remedy, the following would constitute the top-10 questions you should always ask yourself–and answer–before shelling out the benjamins for anything, whether it’s anti-aging cream, a diet fad program, books purporting to tell you secrets your doctor won’t, or jewelry items containing magnets:

1. What is the source Continue reading

The World Will Not End Tomorrow

The world will not end tomorrow.

The Sun will rise on the morning of December 22 and find most of humanity still living. I can say that with a great deal of confidence, though my scientist’s brain tells me I should say the world “probably” won’t end tomorrow. After all, there’s a tiny chance, a minuscule probability…but it’s so small we don’t have to worry about it, just like we don’t have to worry about being struck down by a meteorite while walking down the street. It could happen, but it almost certainly won’t.

My confidence comes from science. I know it sounds hokey, but it’s true. There’s no scientific reason—absolutely none—to think the world will end tomorrow. Yes, the world will end one day, and Earth has experienced some serious cataclysms in the past that wiped out a significant amount of life, but none of those things are going to happen tomorrow. (I’ll come back to those points in a bit.) We’re very good at science, after centuries of work, and the kinds of violent events that could seriously threaten us won’t take us by surprise.

Why the World Won’t End

So where does this stuff come from? Whose idea was it that “the end of the world will be on December 21, 2012″? The culprit, according to those who buy into the idea, is that the end of the world was predicted by the Mayas in their mythology, and codified in their calendar. However, it’s pretty safe to say that the Mayas didn’t really predict the end of the world, even though I don’t know much about the great Mayan civilization that existed on the Yucatan peninsula in what is now Mexico from antiquity until the Spanish conquest.

See this calendar? It’s being touted as a Mayan
calendar in articles about the “end of the world”,
but it ain’t Mayan. It’s an Aztec calendar. Please
don’t mix up civilizations.

The Mayas were the only people in the Americas known to have developed a complete written language, which is part of how we know a lot about them despite their destruction by the hand of European invaders. In particular, we know about their calendar, and the divisions they used. We use what’s called a decimal system for numbers, based on the 10 fingers of our hands. That’s why we break things up into decades (ten years) and centuries (ten decades), as well as a millennium (ten centuries). The Mayas liked different divisions of time: their b’ak’tun is approximately 394 years, and they placed a certain significance on a cycle of 13 b’ak’tuns. (I suspect the Klingon language in Star Trek borrowed some of its vocabulary from ancient Mayan.)

In the “Long Count,” one version of the Mayan calendar known to us, the present world came to be on August 11, 3114 BC. That world will end at the close of the 13th b’ak’tun from that creation day, which happens to be December 21, 2012. However, there’s good reason to think that the Mayas didn’t believe this would be the end of all things: other calendars exist that refer to an even longer span of years, stretching thousands of years into the future!

Even more importantly, though: the Mayan cosmology (their view of the universe) was cyclic, as in many other religions. This world was not the first in this cosmology, and it won’t be the last. In such a view, the true universe is eternal, and the cycles of time are a kind of divine rebooting, which don’t really end anything. The end of the 13th b’ak’tun might be a transformative event in the Maya cosmology, but it’s not the end of the world.

Frankly, I’m not sure why we should care even if the Mayas did believe this was the end of the world. As I said previously, there’s no scientific reason to think the world will end tomorrow. But maybe you might think there’s a non-scientific reason—divine intervention to wipe out the Earth, perhaps. However, I’d venture to guess that most of us don’t adhere to the Mayan religion. Their gods are not the gods most people worship. The prophesied arrival on Earth of Bolon Yookte’ K’Uh, the Nine-Footed God is not something central to my belief system, and probably not yours either.

In fact, millennial thinking is far more a Christian thing than it is a Mayan thing—or frankly most other religions. When people talk about the supposed end of the world tomorrow, they use the Christian terminology: Armageddon (referring to Megiddo, a place in northern Israel, named in the Book of Revelation as the site of the last battle) or the apocalypse (literally the “uncovering”, when all that was hidden becomes revealed). These weren’t concepts in the Mayan religion, and nothing in the Christian religion says the world will end on December 21, 2012.

The World Will End…Eventually

Some say the world will end in fire,
Some say in ice.
From what I’ve tasted of desire
I hold with those who favor fire.
–Robert Frost

Science tells us the world won’t end tomorrow. It also tells us the Mayan cosmology is wrong: time doesn’t go in cycles forever. Earth began 4.5 billion years ago, and will end in about 5 billion years more—at least as a livable world, which is what counts for us. In between its beginning and end, it is defined by cycles: the length of rotation (days) and the time to travel around the Sun (years), with its associated seasons. Other cycles are pretty arbitrary: centuries and b’ak’tuns don’t have any particular significance in terms of astronomical events.

The end of the world as we know it will happen in about 5 billion years, when the Sun ceases fusing hydrogen into helium in its core. When that happens, the Sun will grow into a red giant star, swallowing up Mercury and Venus. Earth probably won’t be devoured, but with the Sun’s surface so much closer, things will become distinctly unpleasant. It’s unlikely the atmosphere or oceans could survive, meaning the end of most life. (Some microbes could probably continue to live underground. That kind of thing is a story for another day.) However, 5 billion years is a long time from now.
Could another cataclysm overtake us before that time? Yes. As you may know, about 65 million years ago, a large asteroid smashed into Earth, an event that at least helped end the reign of dinosaurs, and ushering the extinction of many other species.

Unfortunately, we can’t rule out the possibility that could happen again. There are enough asteroids and comets in our Solar System that could eventually cross orbital paths with Earth; if a large specimen collided with us, it would be devastating.

However, we’re talking about tomorrow. No asteroid will strike Earth on December 21: astronomers keep careful track of everything near our planet, and nothing we know of is on a collision course with Earth for the near future. Asteroids and comets are really the only things we have to worry about doing serious damage for life on Earth, but you can sleep easy tonight and tomorrow night: we’re safe.

If you could somehow see the planets during
daylight hours, here’s how they would
appear tomorrow at noon. There’s no
alignment. (You can see this for yourself
using the free planetarium program
Stellarium.)

Some people have talked about fairly far-fetched ideas: alignments of planets, or lining up Earth, the Sun, and the center of the galaxy. The planets of the Solar System aren’t aligned tomorrow—the image shows where several of them are in relation to the Sun at noon. Jupiter isn’t anywhere close to the planets you see. You’d need a pretty strong imagination to say they’re lined up in any way: while they do lie along a line, that’s the way they always are, since they all orbit the Sun more or less in the same plane. Alignment with the galactic center is even more simple to dismiss: about once a year, the Sun appears aligned with the galactic center in the sky. And nothing happens.

Another explanation I’ve seen involves a mysterious planet called “Nibiru” or “Planet X,” which either will collide with Earth or otherwise generate a baleful influence. Phil Plait, the Bad Astronomer, has a lot about the Nibiru nonsense, so I won’t repeat what he says. Suffice to say Nibiru doesn’t exist: there’s no evidence for it, and (surprise!) it’s not anything that came from Mayan mythology to begin with, so there’s no reason to associate it with a December 21 apocalypse.

A Positive Conclusion

Science, I think, is reassuring in the midst of panic. Why people like to scare themselves and others with misguided ideas of the world’s end, I am not qualified to say. I don’t know how many people are convinced the world will end tomorrow, compared with the number of people who are either wholly skeptical or those who might be a little worried. However, let me reassure you again: the world will not end tomorrow. We can take comfort in the knowledge that December 22 will come, 2012 will end, and a new year—a new cycle—will begin. Any remaking of the world is up to us, so rather than worrying about imaginary apocalypses, let’s commit to improving the lives of those who live on our magnificent planet.

Life and science challenges: flames, Hawkeye, the needle and the damage done

(source)

Of Heroin, Honorable Mentions, and Hawkeye: A day I will never forget

By Double X Science Biology Editor Jeanne Garbarino


“I look forward to seeing you in 3 months when you will be a whole person again.”

Those were my parting words to a special person in my life who was embarking on an undoubtedly difficult journey toward sobriety.  It was only 7:45am on Friday, June 1st, but already I had learned that the strings from a bikini top make a good tourniquet, and I actually held the syringe that, only moments before, contained a bolus of heroin.  I am still trying to believe that this really was the last time.  

As I attempted to wrap my head around what was happening, I remembered a description of a heroin high as told to me by a former addict.  According to this person, being on heroin feels like you’ve been swaddled in a warm blanket, and gently rocked by a loving mother, except the loving mother was actually the devil.  

Though I could never really understand what it feels like to be hooked on heroin, this helped me make some sense of it.  But, as much as I wanted to be sympathetic, I also wanted to grab my friend by the shoulders and scream.  “Why have you done this to yourself?  Why have you done this to us?”  It has truly been a difficult time, watching this person struggle.  And finding out that I can’t control any of it was probably the hardest lesson I’ve ever learned.

Still, life must go on.

I took a few deep breaths, which helped to quiet the tremble, and began to gather my thoughts.  What was it that I had to do today?  As if I flipped some switch, I began to plan out my day – renew my parking permit, finish that Western blot, read that thesis, and get that new post up on the site.  

Then, around 8:15am, I received an unexpected phone call.  It was Liz Bass from the Center of Communicating Science at Stony Brook University.  She was calling to see if I could make Alan Alda’s World Science Festival discussion about the Flame Challenge, which was to occur at 4pm that afternoon.  Not really knowing what was in store, I quickly accepted (um, hello, Alan Alda).  A second phone call about 20 minutes later informed me that I would be joining Alan on stage.  Was this really happening?  In about 30 minutes time, I went from despair to elation.  I also went to the store to buy a skirt since I was already in transit to my lab (and was dressed like a “scientist”).

As I sat on the train, I began to reflect.  Much of my free time during the month of March was dedicated to producing an entry to Alan Alda’s Flame Challenge contest, which, in an effort to raise science communication awareness, asked scientists from all over the world to define a flame to an 11 year old.  Because I enjoy working on a team, I asked my fellow scicommies, Deborah Berebichez and Perrin Ireland, to join me on this endeavor (three times the brain power!).  For several weeks, we worked on the script, and regularly discussed our progress during late night Google hangouts (which is a fantastic way to collaborate).  This was mostly due to the fact that we all have day jobs and obligations outside of work.  Luckily for me, Debbie and Perrin were willing to meet at a time that coincided after my children’s bedtime routine.

This experience was truly fun and rewarding.  Each of us has a certain set of strengths, which when combined, seemed to just synergize.  We literally examined every word in the script to make sure that it was clear, concise, and hopefully captivating.  Furthermore, we wanted to make sure that it was something an 11-year-old would both learn from and enjoy.

But, we did labor over one particular issue, and that was our use of the Bohr Model to represent an atom.  While this model might be commonplace in many classroom textbooks, scientists now know that electrons exist in orbitals, also known as electron clouds, and the calculations to determine the exact location(s) of an electron are based on probability.  Clearly, this was something very different than stating that electrons simply orbit around a nucleus.  

The analogy that electrons travel around the nucleus in the same way that planets travel around the sun is downright inaccurate.  However, this is an analogy that is still commonly used and is, in my opinion, a great example of how we sacrifice accuracy for simplicity.  I believe that this is the greatest challenge for a science communicator.  

As we talked through this issue, we tried to not lose site of the actual mission, which was to explain a flame to an 11 year old.  Would it help our story to break down the currently accepted atomic theory or would it detract from it?  In the end, we decided to keep our atomic structure simple, but noted that it was a simplified version of an atom.  We figured that by having this little disclaimer, it would inform our audience that there is more to it that what we showed, and maybe it would lead them down a road of scientific inquiry.  

Perhaps it was this attention to detail that landed our Flame Challenge video a spot in the top 15 entries (FYI there were close to 900 entries).   Or perhaps it was because our entry was cute and artistic.  Whatever the reason, we proudly accepted our honorable mention, and I was looking forward to discussing our video with the man himself.

Getting back to Friday, June 1st.   I arrived at the Paley Center for Media around 3:30pm (in a new skirt) and was immediately brought up to the 11th floor and into the green room of Alan Alda.  There, I met my fellow awardees (a combination of finalists and honorable mentions), and of course Alan Alda, who was fantastically charming and funny.  We all sat, around an old table, on which was a lovely array of cheese, nuts, banana chips, and get this, Swedish fish!  I don’t know what it was about the Swedish fish, but seeing this candy helped calm my nerves.

Alan helped us all to break the ice, and discussed his plans for the event.  Apparently we would be leading a panel discussion, and I would be on that panel.  On a stage.  In front of a very large audience.  And it was to be webcasted.  So I popped a few of those Swedish fish and told myself to not be nervous.

As my jaw worked to chew those sticky sweet candies, I couldn’t help but think about when I was a kid and how I used to sit with my dad and watch M*A*S*H.  I never would have believed you if you told me that I was going to be hanging out with Hawkeye when I was older.  But, there he was, telling us about the birth of the Flame Challenge.  I was tempted to ask him where Corporal Klinger is these days, but decided that my time would be better spent getting the plan for the panel firmed up in my brain.

After some quick chitchat, we were asked to make our way to the auditorium.  Seating was charted and mics were checked and around 4pm, it all began.  About an hour into it, we were asked to come on stage.  Each of our entries were highlighted, followed by a chance speak our piece.  Add in some Q&A from the audience and the panel discussion was complete.  A hearty round of applause later, I found myself getting whisked away for pictures.  

When the dust began to settle, I grabbed a beer and started to decompress.  I just couldn’t believe how this day turned out, especially given its start.  The stresses my family and I have been dealing with have certainly taken its toll on all of us, and I am grateful for that little dose of Hawkeye to help lighten things up.  I’m not sure if I will ever experience a day like that again, but that’s ok with me.