How fluorescent lights work: quantum mechanics in the home


We have a tendency to think that “quantum mechanics” is synonymous with “out of the ordinary.” I do that, too, since there’s so much strange to talk about: the blurring of particles and waves, the apparent randomness that drove Einstein crazy, and so forth. It’s easy to forget that quantum mechanics also is an everyday matter. The odds are pretty good you’re reading this post on a computer screen (as opposed to a printout), and possibly the light you’re using is fluorescent.


The three major types of lights you can buy are incandescent bulbs, fluorescent lights (including compact fluorescent lights), and light-emitting diodes. Incandescent bulbs are the “normal” type (though they are becoming less so): They light up when an electric current runs through a thin wire made of tungsten, which heats up. The wattage of an incandescent is a measure of how much power it consumes, and most of that power goes to heat, not light, which is why you can burn your hand if you touch a bulb that’s been on any length of time. Because of the wasteful nature of that kind of bulb, a lot of people have made the switch to compact fluorescent lights (CFLs), which don’t run hot and use a lot less power for the same amount of light. And they work by using quantum mechanics!


Of course even incandescent bulbs are quantum-mechanical underneath: after all, everything Continue reading

Making Light in Electronics

By DXS Physics Editor Matthew Francis 

A while back, I wrote about one of the most common ways of making electric light: fluorescent bulbs. Understanding fluorescent lights requires quantum mechanics! While a lot of quantum physics seems pretty removed from our daily lives, it’s essential to most of our modern technology. In fact, reading what I’m writing requires quantum mechanics, since you are using a computer (maybe a handheld computer like an iPad or smart phone, but it’s still a computer) or a printout from a computer.

Modern electronics, including computers and phones, depend on semiconductors. Conductors (like the copper wire in power cords) let electricity flow easily, but semiconductors conduct electricity more reluctantly—but that very reluctance lets us control the flow. While they can’t sustain large currents like conductors can, we can tinker with the chemistry of semiconductors to make them conduct electricity in very precise ways. One of those ways lets semiconductor devices make light: those are known as light-emitting diodes, or LEDs.

You likely have many LEDs in your home: they’re common as indicator lights on appliances, and you might even have LED light bulbs. While they’re pretty expensive right now, the price of LED lights is getting lower all the time, and they have major advantages over both incandescent (old-style) light bulbs and fluorescents. They won’t burn out even as quickly as fluorescent lights (themselves longer-lived than incandescents), and consume less energy. Since they are based on solids rather than gases, they’re not going to break easily, either! But how do they work?

The Electrons in the Band

When I described fluorescent lights in my earlier post, I described how atoms have distinct energy levels inside them, and light is produced when electrons move between those energy levels. Fluorescent lights use gases (generally mercury vapor), so the atoms are relatively widely separated. In solids, including semiconductors, atoms are tightly packed together, forming bonds that don’t break without high pressures or temperatures. In fact, they may also share electrons with each other; a particularly dramatic example of this is in metals, where the electrons in the highest energy levels of the atoms all form a gas that surrounds the atoms. That’s why metals are such good conductors—a little push from a battery or other power source makes those electrons flow in one direction (on average at least), much as a fan creates currents in the air.

Semiconductors are a bit more complicated: their electrons are loosely bound, but still stuck to their host atoms. The way physicists understand this is something known as the band model: just like atoms have energy levels, solids have energy bands. Low energies correspond to electrons stuck to their atoms, which can’t leave; we call these closed shell electrons (for reasons that aren’t important for this particular post). Moderate energies are known as valence electrons, which stay put ordinarily, but can be persuaded to move if given the right incentive. Finally, high energies are conduction electrons, which aren’t tied to a particular atom at all; as their name suggests, they are the ones that carry electric current.

Whether a solid conducts electricity depends on its band structure, and the size of the energy barrier in between the bands, which is called a gap. Large gaps require large energies for electrons to jump them, while smaller gaps are more easily jumped. Conductors have negligible gaps between their valence and conduction bands, while insulators have huge gaps. Semiconductors lie in between; adding extra atoms to a semiconductor can make the gap smaller (a process known as “doping”, which sometimes makes describing it unintentionally funny).

Cars and Roads and Electrons

At low temperatures, semiconductors may not conduct electricity at all, since no electrons can jump the gap into the conduction band. Either warming them up a bit or applying an external electric current gives the electrons the energy they need to move into the conduction band.

I was pondering analogies about band structures to help us understand them, and thought of this one based on cars and roads. Think of closed shells as like parking spaces along a road: cars (which stand in for electrons) are stationary. Valence bands are the slow lane, which is clogged with traffic, so the cars technically can move, but don’t. The conduction bands are fast lanes: cars can really zip, but there’s a traffic barrier between the slow lane and fast lane. (That barrier is the weakest part of my analogy, so remember that we should be thinking of a barrier as something that can be traversed under some conditions but not others.)

One more complication: there are two types of semiconductors, known as n-type and p-type. In n-type, just a few electrons (cars) have access to the conduction band (fast lane) at a time, but in p-type, enough electrons get in to leave holes in the valence band. Applying a current to the semiconductor shifts another valence electron into the hole, but that leaves another hole, and so forth…so it looks like the hole is moving! In fact, physicists refer to this as “hole conduction”, which also sounds odd if you’re not used to it.

Now we’re finally ready to understand LEDs. If you join an n-type semiconductor to a p-type semiconductor, you make something known as a diode. (The prefix di- refers to the number two. If you join three semiconductors, you get a transistor of either the pnp or npn types, depending on the order you use.) The bands (lanes) don’t line up perfectly at the junction: the conduction band in the n-type is generally only slightly higher than the valence band of the p-type, so just a little nudge is needed to move electrons across. This means when they reach the junction between the materials, electrons from the n-type semiconductor can fill the holes on the p-type, which is a decrease in energy. Just as in individual atoms, moving from a higher energy level to a lower energy level makes a photon—and that’s where the LE in the D comes from!

LEDs tend to produce very pure colors, rather than the mixture of colors our eyes perceive as white light. To create LED light bulbs, generally blue LEDs are coated with a phosphorescent material, much like the kind used in fluorescent bulbs. Unlike fluorescents, though, there’s no gas involved, and less heat is lost (though there is still a little bit). Together these factors make LED light bulbs longer-lasting and more efficient even than fluorescents, though currently they are far more expensive.

Despite how common LEDs and other semiconductors are, they’re considered fairly advanced physics. But guess what: if I did my job right, you should understand LED physics now! What is often thought of as “advanced” is really everyday science, and it’s a part of how quantum mechanics (with all its electrons and fascinating interactions on the microscopic level) has helped create our modern world.

Tiptoe through the thalamus…

This is how people looked at the brain in 1673. Things have changed.
Sketch by Thomas Bartholin, 1616-1680. 
Image via Wikimedia Commons. Public domain in USA.
In early October, the Allen Institute for Brain Science dropped a metric buttload of brain data into the public domain.
Founded by Microsoft co-founder Paul Allen, the Allen Institute for Brain Science is, not surprisingly, interested in, um, the brain. Specifically, according to the Institute’s web site, its mission is
“to accelerate the understanding of how the human brain works in health and disease. Using a big science approach, we generate useful public resources, drive technological and analytical advances, and discover fundamental brain properties through integration of experiments modeling and theory.”
Towards that end, researchers at the Allen Institute have been mapping gene expression patterns in the human and mouse brains, as well as neural connectivity in the mouse brain. Why? Well, because as a general rule, science requires a control. If scientists are ever to understand the brain – how we think, how we learn, how we remember things, and how all those processes get scrambled during disease or trauma – they first must understand what a typical baseline brain looks like. The Allen Institute is doing the heavy lifting of mapping out these datasets, one brain slice at a time.
In particular, they are mapping the gene expression and neural connectivity of every part of the brain, so that researchers can identify difference between regions, as well as the physical links that tie them together. Differences in gene expression patterns may reveal, for instance, that seemingly related regions actually have different functions, while connectivity, or brain “wiring,” could shed light on how the brain works. 
I’m a technology nut, so I’m less interested in the answers to these questions than in how we arrive at them. And thanks to the Allen Institute, I (and you) can view these data from the luxury of my very own laptop, no special equipment required. (To be clear, you can’t view the data from my laptop. You’d need my computer, and you can’t have it.) You don’t even need to be a brainiac (I couldn’t help myself) to do it.
Here’s how. Point your browser to http://www.brain-map.org/. From there, choose a dataset – say, “Mouse Connectivity.” This is a dataset of images created by injecting fluorescent tracer molecules into the brains of mice, waiting some period of time, then sacrificing the mice, cutting their brains into thin slices — picture an extremely advanced deli slicer — and taking pictures of each one to see where the tracer material went. The result is a massive collection of images, collected by injecting hundreds of mice, preparing thousands of brain slices, and represents gigabytes upon gigabytes of data, which Allen Institute researchers have then reconstructed into a kind of virtual 3D brain.
In the parlance of neuroscientists, this dataset represents a first-pass attempt at a “connectome” – a brain-wide map of neural connections. But it’s definitely not the last; the connectome is vast beyond reckoning. According to one estimate,
Each human brain contains an estimated 100 billion neurons connected through 100 thousand miles of axons and between a hundred trillion to one quadrillion synaptic connections (there are only an estimated 100–400 billion stars in the Milky Way galaxy).
Efforts are currently underway to map the connectome at a number of levels, from the relatively coarse resolution of diffusion MRI to the subcellular level of electron microscopy. That’s a story for another day, but if you’re interested in this topic, I highly recommend Sebastian Seung’s eminently readable 2012 book, Connectome: How the Brain’s Wiring Makes Us Who We Are.

Back to the Allen Institute datasets. When you click on ‘Mouse Connectivity’, the site presents you with an index of injection sites, 47 in all. Let’s click on “visual areas.” The next page that comes up is a list of datasets that include that region. For the sake of this example, let’s click on the first entry in that list, “Primary visual area,” experiment #100141219.

The resulting page contains 140 fluorescent images of brain tissue slices in shades of orange and green. Click one to see it enlarged. Orange areas are non-fluorescent – they didn’t take up the tracer, meaning they are not physically connected to the injection site. On the bottom of the window is a series of navigation tools – you can tiptoe through the thalamus if you’d like, simply by moving these sliders left-right, up-down, and front-back. Just like a real neuroscientist!
 

This is your brain (well, a mouse brain) on rAAV (a fluorescent tracer).
(Source)

You can also zoom in to the cellular level. Here’s a close-up of a densely fluorescent area of the mouse brain — you can actually see individual neurons in this view. 
 

This is a closeup of your brain on rAAV. (Again, if you were a mouse)
(Source)

Another option is to download the Allen Institute’s free Brain Explorer software, a standalone program that lets you view these data offline. With Brain Explorer you can “step” through the brain slice by slice, rotate it, highlight regions. It’s way cool, even if (like me) you don’t know very much about brain anatomy.
Here’s a screenshot from the application, showing gene expression data in the center of the brain.
 

Screenshot of the Allen Institute’s Brain Explorer software

If you’re interested in how the amazing researchers at the Allen Institute are doing this work, they lay it out for you in a nice series of white papers (here’s the one on the mouse connectivity mapping project). I recommend you take a look!
 
The opinions expressed in this post do not necessarily reflect or conflict with those of the DXS editorial team or contributors.

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 is the sky pink?


On Mars, the sky is pink during the day, shading to blue at sunset. What planet did you think I was talking about?

On Earth, the sky is blue during daytime, turning red at as the sun sinks toward night.

Scattering light

Well, it’s not quite as simple as that: if you ignore your dear sainted mother’s warning and look at the Sun, you’ll see that the sky immediately around the Sun is white, and the sky right at the horizon (if you live in a place where you can get an unobstructed view) is much paler. In between the Sun and the horizon, the sky gradually changes hue, as well as varying through the day. That’s a good clue to help us answer the question every child has asked: why is the sky blue? Or as a Martian child might ask: why is the sky pink?

First of all, light isn’t being absorbed. If you wear a blue shirt, that means the dye in the cotton (or whatever it’s made of) absorbs other colors in light, so only blue is reflected back to your eye. That’s not what’s happening in the air! Instead, light is being bounced off air molecules, a process known as scattering. Air on Earth is about 80% nitrogen, with almost all of the rest being oxygen, so those are the main molecules for us to think about.

As I discussed in my earlier article on fluorescent lights, atoms and molecules can only absorb light of certain colors, based on the laws of quantum mechanics. While oxygen and nitrogen do absorb some of the colors in sunlight, they turn right around and re-emit that light. (I’m oversimplifying slightly, but the main thing is that photons aren’t lost to the world!) However, other colors don’t just pass through atoms as though they aren’t there: they can still interact, and the way we determine how that happens is again the color.

The color of light is determined by its wavelength: how far a wave travels before it repeats itself. Wavelength is also connected to energy: short wavelengths (blue and violet light) have high energy, while long wavelengths (red light) have lower energy. When a photon (a particle of light) hits a nitrogen or oxygen molecule, it might hit one of the electrons inside the molecule. Unless the wavelength is exactly right, the photon doesn’t get absorbed and the electron doesn’t move, so all the photon can do is bounce off, like a pool ball off the rail on a billiards table. Low-energy red photons don’t change direction much after bouncing–they hit the electron too gently for that. Higher-energy blue and violet photons, on the other hand, scatter by quite a bit: they end up moving in a very different direction after hitting an electron than they moving before. This whole process is known technically as Rayleigh scattering, for the physicist John Strutt, Lord Rayleigh.

The blue color of the sky

Not every photon will hit a molecule as it passes through the atmosphere, and light from the Sun contains all the colors mixed together into white light. That means if you look directly at the Sun or the sky right around the Sun during broad daylight, what you see is mostly unscattered light, the photons that pass through the air unmolested, making both Sun and sky look white. (By the way, your body is pretty good at making sure you won’t damage your vision: your reflexes will usually twitch your eyes away before any injury happens. I still don’t recommend looking at the Sun directly for any length of time, especially with sunglasses, which can fool your reflexes into thinking everything is safer than it really is.) In other parts of the sky away from the Sun, scattering is going to be more significant.

The Sun is a long way away, so unlike a light bulb in a house, the light we get from it comes in parallel beams. If you look at a part of the sky away from the Sun, in other words, you’re seeing scattered light! Red light doesn’t get scattered much, so not much of that comes to you, but blue light does, meaning the sky appears blue to our eyes. Bingo! Since there is some green and other colors mixed in as well, the apparent color of the sky is more a blue-white than a pure blue.

(The Sun’s light doesn’t contain as much violet light as it does blue or red, so we won’t see a purple sky. It also helps that our eyes don’t respond strongly to violet light. The cone cells in our retinas are tuned to respond to blue, green, and red, so the other colors are perceived by triggering combinations of the primary cone cells.)

At sunset, light is traveling through a lot more air than it does at noon. That means every ray of light has more of a chance to scatter, removing the blue light before it reaches our eyes. What’s left is red light, making the sky at the horizon near the Sun appear red. In fact, you see more gradations of color too: moving your vision higher in the sky, you’ll note red shades into orange into yellow and so forth, but each color is less intense.

So finally: why is the Martian sky pink? The answer is dust: the surface of Mars is covered in a fine powder, more like talcum than sand. During the frequent windstorms that sweep across the planet, this dust is blown high into the air, where light (yes) scatters off of it. Since the grains are larger than air molecules, the kind of scattering is different, and tends to make the light appear red. (Actually, the sky’s “true” color is very hard to determine, since there is a lot more variation than on Earth.) When there is less dust in the atmosphere, the Martian sky is a deep blue, when the Sun’s light scatters off the carbon dioxide molecules in the air.

By DXS Physics Editor Matthew Francis

Towards better drug development, fewer side effects?

You may have had the experience: A medication you and a friend both take causes terrible side effects in you, but your friend experiences none. (The running joke in our house is, if a drug has a side-effect, we’ve had it.) How does that happen, and why would a drug that’s meant to, say, stabilize insulin levels, produce terrible gastrointestinal side effects, too? A combination of techy-tech scientific approaches might help answer those questions for you — and lead to some solutions.

It’s no secret I love lab technology. I’m a technophile. A geek. I call my web site “Biotechnically Speaking.” So when I saw this paper in the September issue of Nature Biotechnology, well, I just had to write about it.

The paper is entitled, “Multiplexed mass cytometry profiling of cellular states perturbed by small-molecule regulators.” If you read that and your eyes glazed over, don’t worry –- the article is way more interesting than its title. 

Those trees on the right are called SPADE trees. They map cellular responses to different  stimuli in a collection of human blood cells. Credit: (c) 2012 Nature America [Nat Biotechnol, 30:858--67, 2012]
Here’s the basic idea: The current methods drug developers use to screen potential drug compounds –- typically a blend of high-throughput imaging and biochemical assays – aren’t perfect. If they were, drugs wouldn’t fail late in development. Stanford immunologist Garry Nolan and his team, led by postdoc Bernd Bodenmiller (who now runs his own lab in Zurich), figured part of that problem stems from the fact that most early drug testing is done on immortalized cell lines, rather than “normal” human cells. Furthermore, the tests that are run on those cells aren’t as comprehensive as they could be, meaning potential collateral effects of the compounds might be missed. Nolan wanted to show that flow cytometry, a cell-analysis technique frequently used in immunology labs, can help reduce that failure rate by measuring drug impacts more holistically. 


Nolan is a flow cytometry master. As he told me in 2010, he’s been using the technique for more than three decades, and even used a machine now housed in the Smithsonian.


In flow cytometry, researchers treat cells with reagents called antibodies, which are immune system proteins that recognize and bind to specific proteins on cell surfaces. Each type of cell has a unique collection of these proteins, and by studying those collections, it is possible to differentiate and count the different populations.


Suppose researchers wanted to know how many T cells of a specific type were present in a patient’s blood. They might treat those cells with antibodies that recognize a protein known as CD3 to pick those out. By adding additional antibodies, they can then select different T-cell subpopulations, such as CD4-positive helper T cells and CD8-positive cytotoxic T cells, both of which help you mount immune responses.


Cells of the immune system
Source: http://stemcells.nih.gov/info/scireport/chapter6.asp
In a basic flow cytometry experiment, each antibody is labeled with a unique fluorescent dye –- the antibody targeting CD3 might be red, say, and the CD4 antibody, green. The cells stream past a laser, one by one. The laser (or lasers –- there can be as many as seven) excites the dye molecules decorating the cell surface, causing them to fluoresce. Detectors capture that light and give a count of how many total cells were measured and the types of cells. The result is a kind of catalog of the cell population. For immune cells, for example, that could be the number of T cells, B cells (which, among other things, help you “remember” previous invaders), and macrophages (the big cells that chomp up invaders and infected cells). By comparing the cellular catalogs that result under different conditions, researchers gain insight into development, disease, and the impact of drugs, among other things.


But here’s the problem: Fluorescent dyes aren’t lasers, producing light of exactly one particular color. They absorb and emit light over a range of colors, called a spectrum. And those spectra can overlap, such that when a researcher thinks she’s counting CD4 T cells, she may actually be counting some macrophages. That overlap leads to all sorts of experimental optimization issues. An exceptionally talented flow cytometrist can assemble panels of perhaps 12 or so dyes, but it might take months to get everything just right.


That’s where the mass cytometry comes in. Commercialized by DVS Sciences, mass cytometry is essentially the love-chid of flow cytometry and mass spectrometry, combining the one-cell-at-a-time analysis of the former with the atomic precision of the latter. Mass spectrometry identifies molecules based on the ratio of their mass to their charge. In DVS’ CyTOF mass cytometer, a flowing stream of cells is analyzed not by shining a laser on them, but by nuking them in superhot plasma. The nuking reduces the cell to its atomic components, which the CyTOF then measures.

Specifically, the CyTOF looks for heavy atoms called lanthanides, elements found in the first of the two bottom rows of the periodic table, like gadolinium, neodymium, and europium. These elements never naturally occur in biological systems and so make useful cellular labels. More to the point, the mass spectrometer is specific enough that these signals basically don’t overlap. The instrument will never confuse gadolinium for neodymium, for instance. Researchers simply tag their antibodies with lanthanides rather than fluorophores, and voila! Instant antibody panel, no (or little) optimization required.

Periodic Table of Cupcakes, with lanthanides in hot pink frosting.
Source: http://www.buzzfeed.com/jpmoore/the-periodic-table-of-cupcakes
Now back to the paper. Nolan (who sits on DVS Sciences’ Scientific Advisory Board) and Bodenmiller wanted to see if mass cytometry could provide the sort of high-density, high-throughput cellular profiling that is required for drug development. The team took blood cells from eight donors, treated them with more than two dozen different drugs over a range of concentrations, added a dozen stimuli to which blood cells can be exposed in the body, and essentially asked, for each of the pathways we want to study, in each kind of cell in these patients’ blood, what did the drug do?


To figure that out, they used a panel of 31 lanthanides –- 10 to sort out the cell types they were looking at in each sample, 14 to monitor cellular signaling pathways, and 7 to identify each sample.


I love that last part, about identifying the samples. The numbers in this experiment are kind of staggering: 12 stimuli x 8 doses x 14 cell types x 14 intracellular markers per drug, times 27 drugs, is more than half-a-million pieces of data. To make life easier on themselves, the researchers pooled samples 96 at a time in individual tubes, adding a “barcode” to uniquely identify each one. That barcode (called a “mass-tag cellular barcode,” or MCB) is essentially a 7-bit binary number made of lanthanides rather than ones and zeroes: one sample would have none of the 7 reserved markers (0000000); one sample would have one marker (0000001); another would have another (0000010); and so on. Seven lanthanides produce 128 possible combinations, so it’s no sweat to pool 96. They simply mix those samples in a single tube and let the computer sort everything out later.


This graphic summarizes a boatload of data on cell signaling pathways impacted by different drugs.
Credit: (c) 2012 Nature America [Nat Biotechnol, 30:858--67, 2012]
When all was said and done, the team was able to draw some conclusions about drug specificity, person-to-person variation, cell signaling, and more. Basically, and not surprisingly, some of the drugs they looked at are less specific than originally thought -– that is, they affect their intended targets, but other pathways as well. That goes a long way towards explaining side effects. But more to the point, they proved that their approach may be used to drive drug-screening experiments.


And I get to write about it. 

As Seen on TV! Restoring Hair with LASERS!!!!!!

The author’s rapidly-expanding forehead.

Anyone who watches TV, reads magazines, or flips through catalogs has seen some interesting products. Maybe they seem plausible to you, maybe they don’t. However, a little investigation shows they are based less on science and well…actually working, and more on wishful thinking. At worst they’re actual con-jobs, designed to separate you from your money as efficiently as possible (which I guess is a certain standard of success). As a result, we at Double X Science bring you “As Seen on TV!” In these features, we’ll look at some of the products shilled on talk shows and infomercials, items lurking between the articles you read in magazines, or things you might find on the shelves of the stores where you shop.

I admit it, I’m a balding dude. My forehead is gradually taking over my entire scalp, replacing my formerly thick and curly hair with a vast expanse of pink skin. Yes, dear readers: My hair was once so thick and curly that, when I wore it long and in a ponytail, ladies would ask me for my secret. (The answer: Wash it every other day with some brand of cheap shampoo and let it air dry. Don’t tell.) I don’t like the fact of my impending baldness, so I’m sympathetic toward defoliation-sufferers who want to bring their hair back at any cost.

On the other hand, I don’t think I’ll invest in any of the hair restoration products advertised in the SkyMall catalog I picked up on my flight to my brother’s wedding in San Francisco. I counted seven products in this single catalog promising to restore hair in one way or another, either reversing baldness or filling in thin patches on the scalp –- and that doesn’t include hair-coloring, extensions, or other options. I won’t cover all of them, but no fewer than three products pledge to bring hair back through the magic of lasers.

Ah, lasers. They may not have the mystique of magnets or the nous of “natural”, but they are a frequent ingredient in modern snake oil. (Come to think of it, one of the hair-restoration products may have contained snake oil. I don’t want to ask.) But while lasers can help correct nearsightedness in some cases, perform minimally invasive surgeries, and remove hair, color my scalp skeptical about their ability to restore hair.

First, a disclaimer: I’m not a biologist, a doctor, medical researcher, or in any field related to those. I’m a physicist, so the closest I ever get professionally to this topic is the “no-hair” theorem in black hole physics. The “no-hair” theorem says that black holes have very few distinguishing characteristics: only mass and rotational rate (and technically electric charge as well, though it’s hard to build up enough charge to make a difference). The analogy is that, if all humans were completely hairless, we would have a lot fewer ways to tell each other apart. In other words, this ain’t my area, so bear (bare) with me!

Night on Baldhead Mountain

Hair loss can occur for a wide variety of reasons: chemotherapy, a number of unrelated diseases, even stress. However, as humans (both men and women!) age, we all tend to lose our hair to some degree. The effect is most pronounced in male pattern baldness (a bare patch on the top of the head merging over time with the growing forehead to leave a fringe around the edges of the scalp) or female pattern baldness (a general loss of hair at the top of the scalp). However, past the age of 80, nearly everyone starts losing hair, regardless of genetics, diet, or health.

The reasons, as with so many other things, are hormonal. Hair production is governed by sex hormones: most famously testosterone, but also a less well-known cousin known as dihydrotestosterone (DHT). In some people, DHT commands the follicles — the small organs in the skin that produce and feed hair — to shrink, producing ever-finer hair until they cease operating entirely. Thus, gradual hair loss of the usual (as opposed to disease- or circumstance-derived) variety is generally preceded by the hair itself becoming thinner and fuzzier.

My naive understanding of the biology of hair loss leads me to suspect that since hormones are the culprit behind hair loss, then any hair restoration should address those hormones in some way. That alone makes me suspicious of the laser-based products SkyMall peddles. To see why, let’s look at lasers themselves.

Lasers (without sharks)

The word “laser” began as an acronym: Light Amplification by the Stimulated Emission of Radiation. The details could be an Everyday Science or Double Xplainer post in their own right, but here’s the short version. The lasers used in the SkyMall products are LED lasers, meaning they are based on the underlying physics as LED lights. An electric current kicks electrons or other electric charge carriers from one type of material to another across a junction. The excess energy the electric charge sheds during this process is given off in the form of a photon, a particle of light. Since the same amount of energy is involved every time, light from LEDs is nearly monochromatic, meaning it is almost purely one color.

The “amplification” part of the name comes by putting the LED into a special kind of cavity with reflective walls. These walls set up standing waves for the light, which interfere constructively like vibrations in a guitar string, making them brighter. However, unlike guitar strings, the production of the light in lasers is a self-feeding process, resulting in the different parts of the system synchronizing until they emit photons in concert with each other. It’s really interesting stuff, and while it’s somewhat complicated, there’s nothing really mysterious or magical about it, any more than magnets are magical.

In fact, LED lasers are so unmagical that you can buy them as cat toys. LED lasers are the inner workings of laser pointers, which you can buy very inexpensively at any number of shops.

The smell of frying follicles

One of three laser-based hair-restoration products from SkyMall.
This one features built-in headphones, so you can at least listen
to music while you sit around looking like a fool. However,
I recommend a cheaper set of headphones, since the $700
price tag is a bit steep, and you’d get the same result with
regards to hair restoration.
Laser hair removal uses intense lasers to selectively heat the follicles in the skin, hopefully avoiding damage to the rest of the skin. This process can slow down hair growth and cause the hair to fall out of the treated follicles, but it doesn’t always actually stop it: the treatment must be continued for a long term. Basically, the laser is damaging the follicle.

As you can imagine, that also makes me skeptical that lasers can stimulate new hair growth. Lasers produce light…and that’s it! In addition to the usual red lasers like in laser pointers, manufacturers also make infrared lasers, which are useful for surgery. While we perceive infrared as heat (which is why sunshine feels warm), I don’t think merely warming the scalp is going to make hair grow faster, or else you wouldn’t need lasers at all — an electric blanket would do just as well. Too much heating and we’re back at laser hair removal.

Similarly, visible-light lasers like the kind that seem to be in these SkyMall products simply produce red light. Because ordinary light bulbs produce a broad range of colors (white light is a mixture of all the visible-light wavelengths), sitting under a desk lamp would expose your scalp to red light. Yes, it wouldn’t be as intense as lasers, but you could do the same trick with a laser pointer from Schtaples (the Scmoffice Schmupply Schtore), provided you have the patience to hold it against your scalp for long periods of time.

The author engages in home laser hair restoration, while his cats
meow around his feet.
So, to summarize:
  • Hair loss in its most common forms is hormonal, so it’s unclear to me that light (whether laser or otherwise) has anything to do with it. Hair removal can be achieved with lasers, but that involves causing damage to hair follicles, not using anything intrinsic to light.
  • Lasers are simply very monochromatic light sources, that use synchronization of atoms on the microscopic level to do their business. There’s nothing in a laser that isn’t in ordinary light bulbs, though you can make things far more intense with a laser. However, high intensity brings us back to laser hair removal, not restoration.
  • As always, if a product sounds miraculous, it’s probably bunkum. If all it took to regrow hair was a glorified laser pointer, nobody would be bald! LED lasers are cheap and ubiquitous; we could all restore our hair without paying a company $700 (and listen to the music on inexpensive headphones, to boot).
Now if you’ll pardon me, I’ll get back to shining this laser pointer at my scalp.