So What’s the Big Deal About the Higgs Boson, Anyway? A Physics Double Xplainer

The ATLAS detector at the Large Hadron Collider, one of four
detectors to discover a new particle.
By Matthew Francis, physics editor

After decades of searching and many promising results that didn’t pan out, scientists working at the Large Hadron Collider in Europe announced Wednesday they had found a new particle. People got really excited, and for good reason! This discovery is significant no matter how you look at it: If the new particle is the Higgs boson (which it probably is), it provides the missing piece to complete the highly successful Standard Model of particles and interactions. If the new particle isn’t the Higgs boson, well…that’s interesting too.

So what’s the big deal? What is the Higgs boson? What does Wednesday’s announcement really mean? What’s the meaning of life? Without getting too far over my head, let me try to answer at least some of the common questions people have about the Higgs boson, and what the researchers in Europe found. If you’d rather have everything in video form, here’s a great animation by cartoonist Jorge Cham and an elegant explanation by Ian Sample. Ethan Siegel also wrote a picture-laden joyride through Higgs boson physics; you can find a roundup of even more posts and information at Wired and at Boing-Boing. (Disclaimer: my own article about the Higgs is linked both places, so I may be slightly biased.)

Q: What is the Higgs boson?
A: The Higgs boson is a particle predicted by the Standard Model. It’s a manifestation of the “Higgs field”, which explains why some particles have mass and other particles don’t.

Q: Whoa, too fast! What’s a boson?
A: A boson is a large mammal indigenous to North America. No wait, that’s bison. [Ed note: Ha. Ha. Ha.] On the tiniest level, there are two basic types of particles: fermions and bosons. You’re made of fermions: the protons, neutrons, and electrons that are the constituents of atoms are all fermions. On a deeper level, protons and neutrons are built of quarks, which are also fermions. Bosons carry the forces of nature; the most familiar are photons–particles of light–which are manifestations of the electromagnetic force. There are other differences between fermions and bosons, but we don’t need to worry about them for now; if you want more information, I wrote a far longer and more detailed explanation at my personal blog.

Q: What does it mean to be a “manifestation” of a force?
A: The ocean is a huge body of water (duh), but it’s always in motion. You can think of waves as manifestations of the ocean’s motion. The electromagnetic field (which includes stuff like magnets, electric currents, and light) manifests itself in waves, too, but those waves only come in distinct indivisible chunks, which we call photons. The Higgs boson is also a manifestation of a special kind of interaction.

Q: How many kinds of forces are there?
A: There are four fundamental forces of nature: gravity, electromagnetism, and the two nuclear forces, creatively named the weak and strong forces. Gravity and electromagnetism are the forces of our daily lives: Gravity holds us to Earth, and electromagnetism does nearly everything else. If you drop a pencil, gravity makes it fall, but your holding the pencil is electromagnetic, based on how the atoms in your hand interact with the atoms in the pencil. The nuclear forces, on the other hand, are very short-range forces and are involved in (wow!) holding the nuclei of atoms together.

Q: OK, so what does the Higgs boson have to do with the fundamental forces?
A: All the forces of nature have certain things in common, so physicists from Einstein on have tried to describe them all as aspects of a single force. This is called unification, and to this day, nobody has successfully accomplished it. (Sounds like a metaphor for something or other.) However, unification of electromagnetism with the weak force was accomplished, yielding the electroweak theory. Nevertheless, there was a problem in the first version: It simply didn’t work if electrons, quarks, and the like had mass. Because particles obviously do have mass, something was wrong. That’s where the Higgs field and Higgs boson come in. Scottish physicist Peter Higgs and his colleagues figured out that if there was a new kind of field, it could explain both why the electromagnetic force and weak force behave differently and provide mass to the particles.

Q: Wait, I thought mass is fundamental?
A: One of the insights of modern physics is that particles aren’t just single objects: They are defined by interactions. Properties of particles emerge out of their interactions with fields, and mass is one of those properties. (That makes unifying gravity with the other forces challenging, which is a story for another day!) Some particles are more susceptible to interacting with the Higgs. An analogy I read (and apologies for not remembering where I read it) says it’s like different shoes in the snow. A snowshoe corresponds to a low-mass particle: very little snow mass sticks to it. A high-mass particle interacts strongly with the Higgs field, so that’s like hiking boots with big treads: lots of places for the snow to stick. Electrons are snowshoes, but the heaviest quarks are big ol’ hiking boots.

Q: Are there Higgs bosons running around all over the place, just like there are photons everywhere?
A: No, and it’s for the same reason we don’t see the bosons that carry the weak force. Unlike photons, the Higgs boson and the weak force bosons (known as the W and Z bosons — our particle physics friends run out of creative names sometime) are relatively massive. Many massive particles decay quickly into less massive particles, so the Higgs boson is short lived.

Q: So how do you make a Higgs boson?
A: The Higgs field is everywhere (like The Force in Star Wars), but to make a Higgs boson, you have to provide enough energy to make its mass. Einstein’s famous formula E = mc^2 tells us that mass and energy are interchangeable: If you have enough energy (in the right environment), you can make new particles. The Large Hadron Collider (LHC) at CERN in Europe and the Tevatron at Fermilab in the United States are two such environments: Both accelerate particles to close to the speed of light and smash them together. If the collisions are right, they can make a Higgs boson.

Q: Is this new particle actually the Higgs boson then?
A: That’s somewhat tricky. While the Standard Model predicts the existence of a Higgs boson, it doesn’t tell us exactly what the mass should be, which means the energy to make one isn’t certain. However, we have nice limits on the mass the Higgs could have, based on the way it interacts with other particles like the other bosons and quarks. This new particle falls in that range and has other characteristics that say “Higgs.” This is why a lot of physics writers, including me, will say the new particle is probably the Higgs boson, but we’ll hedge our bets until more data come in. The particle is real, though: four different detectors (ATLAS and CMS at CERN, and DZero and CDF at Fermilab) all saw the same particle with the same mass.

Q: But I’m asking you as a friend: Is this the Higgs boson?
A: I admit: a perverse part of me hopes it’s something different. If it isn’t the Higgs boson, it’s something unexpected and may not correspond to anything predicted in any theory! That’s an exciting and intriguing result. However, my bet is that this is the Higgs boson, and many (if not most) of my colleagues would agree.

Q: What’s all this talk about the “God particle”?
A: Physicists HATE it when the Higgs boson is called “the God particle.” Yes, the particle is important, but it’s not godlike. The term came from the title of a book by physicist Leon Lederman; he originally wanted to call it “The Goddamn Particle”, since the Higgs boson was so frustrating to find, but his editor forced a change.

Q: Why should I, as a non-physicist, care about this stuff?
A: While it’s unlikely that the discovery of the Higgs boson will affect you directly, particle colliders like the LHC and Tevatron have spurred development of new technologies. However, that’s not the primary reason to study this. By learning how particles work, we learn about the Universe, including how we fit into it. The search for new particles meshes with cosmology (my own area): It reveals the nature of the Universe we inhabit. I find a profound romance in exploring our Universe, learning about our origins, and discovering things that are far from everyday. If we limit the scope of exploration only to things that have immediate practical use, then we might as well give up on literature, poetry, movies, religion, and the like right now.

Q: If this is the Higgs boson, is that the final piece of the puzzle? Is particle physics done?
A: No, and in fact bigger mysteries remain. The Higgs boson is predicted by the Standard Model, but we know 80% of the mass of the Universe is in the form of dark matter, stuff that doesn’t emit or absorb light. We don’t know exactly what dark matter is, but it’s probably a particle — which means particle colliders may be able to figure it out. Hunting for an unknown particle is harder than looking for one we are pretty sure exists. Finding the Higgs (if I may quote myself) is like The Hobbit: It’s a necessary tale, but the bigger epic of The Lord of the Rings is still to come.

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

Einstein's most famous equation, sort of. This is the transcription of the chalkboard from a public talk Einstein gave in Pittsburgh in 1934. (Credit: Dwight Vincent and David Topper)

Did Einstein write his most famous equation? Does it matter?

Why all the fuss about E = m c2?

By Matthew R. Francis

Albert Einstein in Pittsburgh, 1934. (Credit: Pittsburgh Sun-Telegraph/Dwight Vincent and David Topper)

The association is strong in our minds: Albert Einstein. Genius. Crazy hair. E = m c2. Maybe many people don’t know what else Einstein did, but they know about the hair and that equation. They may think he flunked math in school (wrong, though he did have conflicts with some teachers), that he was a ladies’ man (true, he had numerous affairs during both of his marriages), and that he was the smartest man who ever lived (debatable, though he certainly is one of the central figures in 20th century physics). Rarely, people will remember that he was a passionate antiracist and advocate for world government as a way of bringing peace.

Obviously whole books have been written about Einstein and E = m c2, but a blog post at io9 caught my attention recently. The post (by George Dvorsky) itself looked back to a scholarly paper by David Topper and Dwight Vincent [1], which reconstructed a public lecture Einstein gave in 1934. (All numbers in square brackets [#] are citations to the references at the end of this post.) This lecture was one of many Einstein presented over the decades, but as Topper and Vincent wrote, “As far as we know [the photograph] is the only extant picture with Einstein and his famous equation.”

Well, kind of. The photograph is really blurry, and the authors had to reconstruct what was written because you can’t actually see any of the equations clearly. Even in the reconstructed version (reproduced below)…there’s no E = m c2. Instead, as I highlighted in the image, the equation is E0 = m. Einstein set the speed of light – usually written as a very large number like 300 million meters per second, or 186,000 miles per second – equal to 1 in his chalkboard talk.

Einstein's most famous equation, sort of. This is the transcription of the chalkboard from a public talk Einstein gave in Pittsburgh in 1934. (Credit: Dwight Vincent and David Topper)

Einstein’s most famous equation, sort of. This is the transcription of the chalkboard from a public talk Einstein gave in Pittsburgh in 1934. (Credit: Dwight Vincent and David Topper)

What’s the meaning of this?

It is customary to express the equivalence of mass and energy (though somewhat inexactly) by the formula E = mc2, in which c represents the velocity of light, about 186,000 miles per second. E is the energy that is contained in a stationary body; m is its mass. The energy that belongs to the mass m is equal to this mass, multiplied by the square of the enormous speed of light – which is to say, a vast amount of energy for every unit of mass. –Albert Einstein [2]

Before I explain why it isn’t a big deal to modify an equation the way Einstein did, it’s good to remember what E = m c2 means. The symbols are simple, but they encode some deep knowledge. E is energy; while colloquially that term gets used for a lot of different things, in physics it’s a measure of the ability of a system to do things. High energy means fast motion, or the ability to make things move fast, or the ability to punch through barriers. Mass m, on the other hand, is a measure of inertia: how hard it is to change an object’s motion. If you kick a rock on the Moon, it will fly farther than it would on Earth, but it’ll hurt your foot just as much – it has the same mass and therefore inertia both places. Finally, c is the speed of light, a fundamental constant of nature. The speed of light is the same for an object of any mass, moving at any velocity.

Mass and energy aren’t independent, even without relativity involved. If you have a heavy car and a light car driving at the same speed, the more massive vehicle carries more energy, in addition to taking more oomph to start or stop it moving. However, E = m c2 means that even if a mass isn’t moving, it has an irreducible amount of energy. Because the speed of light is a big number, and the square of a big number is huge, even a small amount of mass possesses a lot of energy.

The implications of E = m c2 are far-reaching. When a particle of matter and its antimatter partner meet – say, an electron and a positron – they mutually annihilate, turning all of their mass into energy in the form of gamma rays. The process also works in reverse: under certain circumstances, if you have enough excess energy in a collision, you can create new particle-antiparticle pairs. For this reason, physicists often write the mass of a particle in units of energy: the minimum energy required to make it. That’s why we say the Higgs boson mass is 126 GeV – 126 billion electron-volts, where 1 electron-volt is the energy gained by an electron moved by 1 volt of electricity. For comparison, an electron’s mass is about 511 thousand electron-volts, and a proton is 938 million electron-volts.

In our ordinary units the velocity of light is not unity, and a rather artificial distinction between mass and energy is introduced. They are measured by different units, and energy E has a mass E/C2 where C is the velocity of light in the units used. But it seems very probable that mass and energy are two ways of measuring what is essentially the same thing, in the same sense that the parallax and distance of a star are two ways of expressing the same property of location. –Arthur Eddington [3]

Another side of the equation E = m c2 appears when we probe the structure of atomic nuclei. An atomic nucleus is built of protons and neutrons, but the total nuclear mass is different than the sum of the masses of the constituent particles: part of the mass is converted into binding energy to hold everything together. The case is even more dramatic for protons and neutrons themselves, which are made of smaller particles knowns as quarks – but the total mass of the quarks is much smaller than the proton or neutron mass. The extra mass comes from the strong nuclear force gluing the particles together. (In fact, the binding particles are known as gluons for that reason, but that’s a story for another day.)

A brief history of an idea

The E0 = m version of the equation Einstein used in his chalk-talk might seem like it’s a completely different thing. You might be surprised to know that he almost never used the famous form of his own discovery: He preferred either the chalkboard version or the form m = E/c2. In fact, in his first scientific paper on the subject (which was also his second paper on relativity), he wrote [4]:

If a body gives off the energy L in the form of radiation, its mass diminishes by L/c2. The fact that the energy withdrawn from the body becomes energy of radiation evidently makes no difference, so that we are led to the more general conclusion that … the mass of a body is a measure of its energy-content …

In other words, he originally used L for energy instead of E. However, it’s equally obvious that the meaning of E = m c2 is present in the paper. Equations, like sentences in English, can often be written in many different ways and still convey the same meaning. By 1911 (possibly earlier), Einstein was using E for energy [5], but we can use E or L or U for energy, as long as we make it clear that’s what we’re doing.

The same idea goes for setting c equal to one. Many of us are familiar with the concept of space-time: that time is joined with space (thanks to the fact that the speed of light is the same, no matter who measures it). We see the blurring of the boundary between space and time when astronomers speak of light-years: the distance light travels in one year. Because c – and therefore c2 – is a fixed number, it means the difference between mass and energy is more like the difference between pounds and kilograms: one is reachable from the other by a simple calculation. Many physicists, including me, love to use c = 1 because it makes equations much easier to write.

In fact, physicists (including Einstein) rarely use E = m c2 or even m = E/c2 directly. When you study relativity, you find those equations are specific forms of more general expressions and concepts. To wit: The energy of a particle is only proportional to its mass if you take the measurement while moving at the same speed as the particle. Physical quantities in relativity are measured relative to their state of motion – hence the name.

That’s the reason I don’t care that we don’t have a photo of Einstein with his most famous equation, or that he didn’t write it in its familiar form in the chalk-talk. The meaning of the equation doesn’t depend on its form; its usefulness doesn’t derive from Einstein’s way of writing it, or even from Einstein writing it.

A small representative sample of my relativity books, with my cats Pascal and Harriet for scale.

A small representative sample of my relativity books, with my cats Pascal and Harriet for scale.

Even more: Einstein is not the last authority on relativity, but the first. I counted 64 books on my shelves that deal with the theory of relativity somewhere in their pages, and it’s possible I missed a few. The earliest copyright is 1916 [6]; the most recent are 2012, more than 50 years after Einstein’s death. The level runs from popular science books (such as a couple of biographies) up to graduate-level textbooks. Admittedly, the discussion of relativity may not take up much space in many of those books – the astronomy and math books in particular – but the truth is that relativity permeates modern physics. Like vanilla in a cake, it flavors many branches of physics subtly; in its absence, things just aren’t the same.

References

  1. David Topper and Dwight Vincent, Einstein’s 1934 two-blackboard derivation of energy-mass equivalence. American Journal of Physics75 (2007), 978. DOI: 10.1119/1.2772277 . Also available freely in PDF format.
  2. Albert Einstein, E = mc2. Science Illustrated (April 1946). Republished in Ideas and Opinions (Bonanza, 1954).
  3. Arthur Eddington, Space, Time, and Gravitation (Cambridge University Press, 1920).
  4. Albert Einstein, Does the inertia of a body depend upon its energy-content? (translated from Ist die Trägheit eines Körpers von seinem Energiegehalt abhängig?). Annalen der Physic17 (1905). Republished in the collection of papers titled The Principle of Relativity (Dover Books, 1953).
  5. Albert Einstein, On the influence of gravitation on the propagation of light (translated from Über den Einfluss der Schwerkraft auf die Ausbreitung des Lichtes). Annalen der Physic35 (1911). Republished in The Principle of Relativity.
  6. Albert Einstein, Relativity: The Special and the General Theory (1916; English translation published by Crown Books, 1961).

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:

[<a href="http://storify.com/fiainros/double-x-science-panel-at-geekgirlcon-2012" target="_blank">View the story "Double X Science panel at GeekGirlCon 2012" on Storify</a>]

Photo by Adrienne Roehrich and used with permission.

Posted by Adrienne M. Roehrich, Chemistry Editor

How helpful are dense-breast right-to-know laws?

A doctor reviews a digital mammogram, pointing to a possible cancer.
Credit: National Cancer Institute.
By Laura Newman, DXS contributor
In a victory for the dense-breast patient movement, Governor Jerry Brown (D-CA) signed legislation last week requiring that doctors who discover that women have dense breasts on mammography must inform women that:

§  dense breasts are a risk factor for breast cancer;
§  mammography sees cancer less well in dense breasts than in normal breasts; and
§  women may benefit from additional breast cancer screening.

The California law goes into effect on April 1, 2013. It follows four states (Connecticut, Texas, Virginia, and New York) with similar statutes. All have enjoyed solid bipartisan support. Rarely do naysayers or skeptics speak up.
Young women who are leading the charge often bring lawmakers the story of a young constituent, diagnosed with a very aggressive, lethal cancer that was not shown on film-screen mammography. The Are You Dense? patient advocacy group engages patients on Facebook, where women share their experiences with breast cancer, organize events, and lobby for legislation. Individual radiologists work with the advocacy groups, but many radiology groups and breast surgeons do not endorse these laws.


A Closer Look at Breast Cancer Data

Living in an age when information is viewed as an entitlement, knowledge, and power, many physicians find it hard to argue against a patient’s right to know. Can sharing information be a mistake? Some epidemiologists think so. Otis W. Brawley, MD, FACP, Chief Medical & Scientific Officer, American Cancer Society, says: “I really worry when we legislate things that no one understands. People can get harmed.” Numerous issues have to be worked out, according to Brawley. For one, he explains: “There is no standard way to define density.” Additionally, “even though studies suggest that density increases the risk of cancer, these cancers tend to be the less serious kind, but even that is open to question,” Brawley says. “We in medicine do not know what to do for women who have increased density.”

A study of more than 9,000 women in the Journal of the National Cancer Institute revealed that women with very dense breasts were no more likely to die than similar patients whose breasts were not as dense. “When tumors are found later in more dense breasts, they are no more aggressive or difficult to treat,” says Karla Kerlikowske, MD, study coauthor, and professor of medicine and epidemiologist at the University of California San Francisco. In fact, an increased risk of death was only found in women with the least dense breasts.


The trouble is what is known about dense breasts is murky. Asked whether he backs advising women that dense breasts are a risk factor for breast cancer, Anthony B. Miller, MD, Co-Chair of the Cancer Risk Management Initiative and a member of the Action Council, Canadian Partnership Against Cancer, and lead investigator of the Canadian National Breast Cancer Screening Study, says: “I would be very cautious. The trouble is people want certainty and chances are whatever we find, all we can do is explain.”

Women in their forties, who are most likely to have dense breasts (density declines with age) may want to seek out digital mammography. In studies comparing digital mammography to film-screen mammography in the same women, digital mammography has been shown to improve breast cancer detection in women with dense breasts. Findings from the Digital Mammographic Imaging Screening Study, showed better breast cancer detection with digital mammography. But digital mammography is not available in many areas.  Moreover, Miller explains: “We do not know if this will benefit women at all.  It is very probable that removal of the additional small lesions will simply increase anxiety and health costs, including the overdiagnosis of breast cancer, and have no impact upon mortality from breast cancer.”


Additional imaging studies sound attractive to people convinced that there is something clinically significant to find. But as I pointed out in my last post, many radiologists and breast physicians contend that there is no evidence that magnetic resonance imaging or any other imaging study aids breast cancer screening in women with dense breasts. Brawley notes: “These laws will certainly lead to more referral for MRI and ultrasound without clear evidence that women will benefit (lives will be saved.) It’s clear that radiologists will make more money offering more tests.” Miller adds: “A number of doctors are trying to capitalize on this and some of them should know a lot better.”


Many Advocates Question More Tests, Statutes

Even though the “Are You Dense?” campaign has been instrumental in getting legislation on the books across the county, other advocacy groups and patient advocates want research, enhanced patient literacy about risks and benefits of procedures. Many recall mistakes made that led women down the path of aggressive procedures. In that group is the radical Halsted mastectomy, used widely before systematic study, but once studied,  found no better than breast-conserving surgery for many cancers, and bone marrow transplants, also found to be ineffective, wearing, and costly.

Jody Schoger, a breast cancer social media activist at @jodymswho engages women weekly on twitter at #bcsm, had this to say on my blog about the onslaught of additional screening tests:

“What is needed is not another expensive modality… but concentrated focus for a biomarker to indicate the women who WILL benefit from additional screening. Because what’s happening now is an avalanche of screening, and its subsequent emotional and financial costs, that is often far out of proportion to both the relative and absolute risk for invasive cancer. I simply don’t think more “external” technology is the answer but one that evolves from the biology of cancer.”

Eve Harris @harriseve, a proponent of patient navigation and patient literacy, challenged Peter Ubel, MD, professor of business administration and medicine, at Duke University, on his view of the value of patient empowerment on the breast density issue. In a post on Forbes, replicated in Psychology Today, Ubel argued that in cases where the pros and cons of a patient’s alternatives are well known, for example, considering mastectomy or lumpectomy, patient empowerment play an important role. “But we are mistaken to turn to patient empowerment to solve dilemmas about how best to screen for cancer in women with dense breasts,” he writes.


Harris disagrees, making a compelling case for patient engagement:

“I think that we can agree that legislative interference with medical practice is not warranted when it cannot provide true consumer protection. But the context is the biggest culprit in this situation. American women’s fear of breast cancer is out of proportion with its incidence and its mortality rate. Truly empowering people—patients would mean improving health literacy and understanding of risk…”


But evidence and literacy take time, don’t make for snappy reading or headlines, and don’t shore up political points. Can we stop the train towards right-to-inform laws and make real headway in women’s health? Can we reallocate healthcare dollars towards effective treatments that serve patients and engage them in their care? You have to wonder.
[Today's post is from Patient POVthe blog of Laura Newman, a science writer who has worked in health care for most of her adult life, first as a health policy analyst, and as a medical journalist for the last two decades. She was a proud member of the women’s health movement. She has a longstanding interest in what matters to patients and thinks that patients should play a major role in planning and operational discussions about healthcare. Laura’s news stories have appeared in Scientific American blogs, WebMD Medical News, Medscape, Drug Topics, Applied Neurology, Neurology Today, the Journal of the National Cancer Institute, The Lancet, and BMJ, and numerous other outlets. You can find her on Twitter @lauranewmanny.]

The opinions in this article do not necessarily conflict with or reflect those of the DXS editorial team. 

Think pink? I’d rather raise a stink

Are some of these possible signs of breast cancer present
in a famous work of art? Image: public domain, US gov
by Liza Gross, contributor
[Ed. note: This article was originally posted on KQED QUEST on October 3, 2012. It is reposted here with kind permission.]
Just a generation ago, October belonged to the colors of fall, when “every green thing loves to die in bright colors,” as Henry Ward Beecher said. (Growing up back East, you read a lot of odes to fall foliage in school.) For years after moving to the Bay Area from Pennsylvania, I felt a twinge of melancholy when October rolled around, knowing the once-demure woodlands would let loose in a fleeting blaze of brash reds and orange-tinged yellows without me.
Now, of course, October belongs to all things pink, as high-profile outfits from the NFL to Ace Hardware set aside 31 days to raise awareness and money for Breast Cancer Awareness Month. (National Breast Cancer Awareness Month was launched in 1985 by CancerCare, a nonprofit cancer support group, and cancer-drug maker AstraZeneca.)
But as women’s health advocate Dr. Susan Love says, awareness of the disease isn’t the issue. “When the NFL is wearing pink gloves, I think you can say we’re aware,” she said last year. “But the awareness isn’t enough.”
Even raising money isn’t enough. You have to ask where that money is going.
It’s a message that gets lost in an ocean of pink-ribbon products (from bagels and teddy bears to vodka and wine glasses), even though critics like the San Francisco-based nonprofit Breast Cancer Action have warned about “pinkwashing” for years, urging people to look behind the feel-good messages to see who’s really benefiting from the commercialization of cancer.
Breast Cancer Action’s Think Before You Pink—Raise a Stink! campaign encourages consumers to think critically about pink products and ask four simple questions to find out what proportion of proceeds go to breast cancer programs and whether the products sold are safe. The group has especially targeted cosmetics companies for marketing pink merchandise even as they sell products with toxic ingredients. (For more information, download the group’s 30-page “toolkit”.)
The group also urges companies to be more transparent and has long called out those it believes use a good cause to increase their bottom line.
Like Eureka, which donated a dollar for every vacuum cleaner sold in its “Clean for the Cure” campaign. Or American Express, which donated a penny per transaction in its “Charge for the Cure.” Both companies bowed out of the pink sweepstakes after Breast Cancer Action asked just how breast cancer patients were benefiting from the campaigns in a 2002 ad in the New York Times.


In October 2000, the San Francisco-based advocacy group 

Breast Cancer Action ran a full page ad in the New York Times 
West Coast Edition with text (not shown) inviting readers to 
participate in its ”Stop Cancer Where It Starts” Campaign. 
The campaign criticized breast cancer awareness campaigns 
for pushing early detection and mammograms 
(without acknowledging their limitations) while ignoring prevention. 
(Image: Courtesy Breast Cancer Action)

Others, like KFC with its 2010 “Buckets for the Cure” campaign, climb on the pink bandwagon to peddle decidedly unhealthy products. Stephen Colbert’s take on the “pink bucket dilemma” shows just how ludicrous cause marketing has become. (Forward to 1:13.)

But even when money goes to breast cancer programs and not corporate coffers, is it going to the right place? Love (and several advocacy groups) has said for years that we need to shift our focus from cures to causes—and prevention.
If we can develop a vaccine for cervical cancer, says Love, why not for breast cancer? Early results of a clinical trial show promising results for a vaccine designed to prevent recurrence of one form of breast cancer. (The data were presented at a meeting and have not yet gone through peer review.)
As I wrote in May, Love’s Research Foundation is looking for volunteers in her online Army of Women to identify potential causes in order to eradicate the disease. (Anyone can sign up.)


In the late 1990s, The Breast Cancer Fund, the American Cancer Society, 

and the Susan G. Komen Breast Cancer Foundation invited American 
artists and writers to submit work about their breast cancer experiences. 
The resulting exhibit (and book)—Art.Rage.Us.—opened in 1998 
at San Francisco’s Main Library. At the time, project coordinator and 
Breast Cancer Action Co-founder Susan Claymon said, 
“Art.Rage.Us. presents deeply moving and beautiful expressions 
from women with breast cancer, along with intensely personal 
statements that provide a window into their hearts and minds.” 
Claymon died of breast cancer in 2000. She was 61.

Prevention is also a primary concern for the Athena Breast Health Network, a partnership of the five University of California medical centers that collects personalized data on breast cancer patients to optimize treatment and ultimately figure out how to stop cancer before it starts. The site also includes a comprehensive list of breast cancer risk factors.

Recent research suggests that the biology behind one of the listed risk factors, dense breast tissue, may be more complicated than previously thought. Earlier studies found that women with dense breasts had a higher risk of developing breast cancer. (And this finding led to the“right to know” legislation that Gov. Brown recently signed, requiring doctors to tell women if their mammograms show they have dense breasts.) But a recent study in the Journal of the National Cancer Institute suggests that women with denser breasts are not more likely to die of breast cancer. The greatest risk was found for women who had the fattiest breast tissue, a condition linked to obesity. This suggests that if you have dense breast tissue, you may be more likely to get cancer—but not die of it. Love’s blog explained the significance of the findings:
The recent study on breast density showed us, yet again, that women who are obese when they are diagnosed with breast cancer are more likely to die of breast cancer than women who are not obese. Doctors need to do more than tell women about their breast density or remind them to get a mammogram. They need to be teaching women the importance of exercising, losing weight (if necessary) and eating a well-balanced diet—both before and after a breast cancer diagnosis. Continue reading