E. coli Up Close and Personal: Scientific Rockstar and Public Enigma

It seems nothing puts fear in the hearts of the masses like mentioning E. coli. Most think of the disease-causing germ that contaminates everything from spinach to beef. I agree the strain Escherichia coli O157:H7 and its cousins O26, O145, STEC O104:H4, and others, are a wretched bunch that give the whole species a bad reputation. What makes these strains so vile are the extra proteins encoded within their genome. For example, E. coli O157:H7 has a larger genome coding for 5561 proteins while the parent strain E. coli W codes for 4739 proteins. Thus is the life of a bacterium. The fact there are so many bacteria means they are usually in close proximity to each other. Physical contact between bacteria, not just those of the same species, allows for the transfer of genetic material between two cells (horizontal gene transfer); the closest thing to sexual reproduction you will find for prokaryotes. If the genes transferred to the recipient give it an advantage or new ability that helps it compete and thrive in its environment, they will remain in the genome. Otherwise, they will be discarded after genome compaction.

Most E. coli are completely harmless and, in fact, beneficial. If the general public knew more than what was broadcasted on the 24 hour news channels, they would see the tiny rockstar scientists have known about for some time now. Beginning in earnest in the 1950s, E. coli is easily cultured in laboratories and very cheaply. Its quick generation time (20 min. at optimum temperature) made it a great model organism to study in many fields of science and medicine. This organism is the work horse of biotechnology due to the relative ease of manipulating its genome or adding complete genetic circuits into the cell using plasmids.


Even after 50 years of intense research, E. coli still holds many unknowns out of the reach of our knowledge. Like all other sequenced genomes, there are a number of “hypothetical proteins” and “proteins of unknown function”. This means by our best abilities, we can locate parts of the genome that code for proteins, however, this doesn’t mean we are able to understand the function of a particular protein.

Image courtesy of Predrag Radivojac. Thanks, Pedra.

The above shows just how much work is left to understand the biological capabilities of Mother Nature. Short version: over 40 gene sequences in databases, but the number of which that we know what the function is holding steady around 500,000 and the number of solved protein structures is over 100,000. This is a growing gap between the known and unknown.

 Where would we be without E. coli?

One advantage of E. coli is their effect on our immune system. Some may find this counter-intuitive, but E. coli can lower the workload of our immune system when pathogens are present, especially in the intestine. When E. coli attach to the GI wall, it changes the acidity of the lining thus making infection from other bacteria less likely. Another benefit is in overall digestion. E. coli promotes better breakdown of food thus preventing accumulation of waste which is a major cause of bloating and constipation.

Many outside the scientific community may not be aware of how integral E. coli are to the advancement of many fields including medicine, pharmacology, biology, and even human physiology. Another reason to not believe the hype.

An Open Letter to the Science Channel

Dear Science Channel,

First, let me thank you for the countless hours of edutainment you have provided me over the years. They have been informative and helped me visualize this universe in many ways. Over the past several months or so, I have noticed something…a trend really…about your content; it is almost entirely focused on the field of physics. I am not complaining about this great content since we would not be here without it. However, as a trained biochemist, I find myself extremely jealous of the exposure given to all-things-space-related.

Biology Matters

I agree on the premise that we would “not be here” if not for the physical forces woven by Mother Nature. But, we would also not be here if it were not for the majestic ways matter interacts throughout the universe. No where is this more noticeable than in biology. Biology at all levels requires the interactions of everything, living or not, that are found at levels below. For example, the biomolecules found in all living organisms are only relevant due to the fundamental interactions of the elements which these molecules are composed of. I know this is a chicken vs. egg gripe. Without physics, there is no biology, and without biology, we could not show stellar programming (pun intended) about our universe.

Physics is Mother Nature’s love letter written in the language of mathematics. But science does not have large to be worth attention. Every living cell has a million stories, all worthy of being described and narrated by Mike Rowe.

We are star stuff, but the star stuff becomes much more when everything comes together, interacts, and forms the recipe for Life. This is what many are searching for in outer space, right? Why not focus a bit more on what we do know exists…us.


Matt Russell, Ph.D.

Soil: an under-appreciated dynamic consortium of communities.

Azospirillum brasilense electron micrograph

Quick fact: the amount of data generated by analyzing the genetic make-up of 1 gram of soil would surpass the total for the entire Human Genome Project. That is because a gram of soil may contain between 2,000 and 18,000 different genomes comprised within roughly 40,000,000 to 2,000,000,000 bacteria cells (1) and (2). Soil; we all walk on it, but do we ever think about what might be lurking in it? My daughter does, for instance, because she looks for tiny black snails to bring into our house and put in potted plants. However, I’m referring to things much smaller and much more influential to the overall ecosystem. Bacteria and fungi have mostly beneficial impacts on the lives of plants, but we know only a fraction of a fraction of the total species present. Many of us think of soil as dirt; dry and inorganic, but soil is a dynamic matrix of clay, sand, and silt particles with a mix of decomposing matter and living organisms. The surfaces of these particles make good niches for bacteria to live if they can survive the extreme variation in water and nutrient availability due to the wet/dry cycle.

Soil is a vast reserve of organic carbon, but only a fraction is usable due to decomposition of most carbon into hummus. So, bacteria and other microorganisms are in eternal competition with each other for precious nutrients in their microenvironments. This makes life arduous for soil organisms that are loners or isolated from good sources of nutrients. This is one reason the root zones of plants are like retirement communities to bacteria and fungi; and the plants know it.

Plants are like shipwrecked sailors stranded on a desert island. They have no where to go if conditions change. To help themselves out, they recruit bacteria and fungi to live on, or within, their roots by excreting valuable nutrients into the soil. Surrounding microorganisms take to this like sharks to blood which is what the plants want and need. These bacteria and fungi offer several advantages to plants. First, they can simply take up space; space that plant pathogens would like to inhabit. On top of this, the good bacteria can readily produce antibiotics to kill off any pathogens that might kill their food source. Second, many of these bacteria have the genetic machinery to produce a class of plant hormones called auxins, derivatives of the amino acid tryptophan. Auxin is like human growth hormone. When the bacteria excrete auxin, the plants take it in because it is a cue to increase water and nutrient uptake. So, plants increase nutrient uptake, become healthier and bigger, and by default excrete larger amounts of nutrients for the bacteria. Genius.

The third reason plants attract bacteria is because plants have a big problem; they can’t make useful sources of nitrogen out of thin air. Luckily, many soil bacteria can, and it’s called nitrogen fixation. These bacteria are able to take nitrogen gas from the air and convert it into a form useful to both plant and bacterium: ammonium. This is an energetically expensive process for the bacterial cell. So, in order to make it as easy as possible on the bacteria, plants will protect the cells from nitrogen fixation inhibitors like oxygen and provide essential carbon in the form of amino acids. For this to happen, the bacterial cell literally crawls inside the root cell and becomes a bacteroid encapsulated within a special structure, a nodule, and ultimately becoming an endosymbiont.

And you thought only mammals had beneficial internal bacterial ecosystems. Just like humans, plants would be in a sorry state if it were not for the bacteria that they associate with. I haven’t even touched upon the benefits of fungi, but I’m definitely not a fungal expert. Any takers?


(1) How Deep Is Soil? Daniel D. Richter and Daniel Markewitz BioScience , Vol. 45, No. 9 (Oct., 1995), pp. 600-609

(2) Paul, E. A. & Clark, F. E. Soil microbiology and biochemistry (Academic Press, San Diego,1989).

How Do Bacteria Make Decisions?

Decision making is not limited to animals like humans or birds. Bacteria also make decisions with intricate precision. Imagine being so tiny that you are literally moved by water molecules bumping into you. This is what bacteria encounter perpetually. Now, imagine having no eyes, no ears, no sense of touch, no taste or nose. How would you know what or who was around you? How would you find food now as compared to where you were a short time ago? This is where being able to sense important things like a food source is critical. Bacteria have this on their “mind” all the time. Depending on the size of a bacterium’s genome, these tiny organisms have the ability to sense hundreds to thousands of internal and external signals like carbon sources, nitrogen sources, and pH changes. If these bacteria are motile (able to move around), they can compare how conditions are for them now against how they were a few seconds ago. That’s right, bacteria have a memory albeit short. If conditions are better, they can continue to move in a forward direction. If conditions are worse compared to a few seconds earlier, they can change direction and continue searching for better conditions in their environment to generate energy. But, how do they decide?

I will focus on a lesser known bacterium as my example since I have the most knowledge about it. Azospirillum brasilense is found in the soil around the world and interacts with the roots of cereal plants like corn and wheat. A. brasilense is almost always (except when attached to plant roots) motile and searching for the best niche to provide energy for the cell. This bacterium can “make” its own usable form of nitrogen from nitrogen gas in the air through a process known as nitrogen fixation. This costs the cell a lot of energy so they are searching for nitrogen sources as well as the necessary carbon sources for life. The microscopic world can be cut throat. Having the ability to sense a greater variety of food compounds could mean the difference between being the predominant species in town or being on the fringe.

Back to the question about how these cells decide which direction to travel. One way is through a dedicated group of proteins that regulate how often the cell switches direction. This group of proteins control chemotaxis, the movement of a cell in response to chemicals within their environment. The number of chemotaxis genes varies depending on the complexity of metabolism for a bacterium. The champion at the moment is 129 fromPseudomonas syringae pv. oryzae str. 1_6. The proteins that actually sense the chemical signal are called methyl-accepting chemotaxis proteins (MCPs) or chemoreceptors. Azosprillum brasilense has 48 MCPs within its genome. This does not mean, however, that A. brasilense cells can only sense 48 different chemicals. Most, but not all, of these MCPs don’t interact with the chemicals themselves but sense the changes in the amount of energy the cell has within the environment they reside. If things are good, the MCPs are inactive. However, if energy levels are lower than they were a few seconds before, the MCPs become active and begin the signal to change direction. And these MCPs are VERY sensitive to changes. For example, if the A. brasilense cells are swimming in a liquid medium with 1,000 molecules of sugar, they will detect changes of addition or removal of a few sugar molecules in the medium. Now, move these cells immediately into a medium with 1,000,000,000,0000 sugar molecules and they still will be able to detect removal or addition of a few sugar molecules. This is called adaptation and allows the cells to remain sensitive no matter the concentrations of compounds they encounter.

This beautiful figure shows where different chemotaxis proteins are found within an E. coli cell at stunning resolution. From Greenfield D, McEvoy AL, Shroff H, Crooks GE, Wingreen NS, et al. (2009) Self-Organization of the Escherichia coli Chemotaxis Network Imaged with Super-Resolution Light Microscopy. PLoS Biol 7(6): e1000137. doi:10.1371/journal.pbio.1000137

MCPs by themselves would be useless if they did not interact with some other cellular machinery. Lucky for bacteria, the MCPs are only the first of many specialized proteins for regulating direction of travel. If a chemical binds to an MCP outside the cell, how does the inside of the cell get the message? When chemicals bind to an MCP or stop binding to it, it slightly changes the structure of the MCP. It is thought association or dissociation of chemicals to MCPs causes a rotation like a slight turn of a door knob. Depending on if the MCPs are rotated or not changes the activity of another enzyme that interacts with MCPs, a protein called CheA (pronounced, ‘key A’). When CheA is active, it converts two other proteins into an active form, CheB and CheY. Confused yet? When CheY is in its active form, it interacts with the base of the flagellumand causes the flagellum to switch direction of rotation and causes the bacterium to change the direction it is moving. The take home message for the mechanism is this: when the MCPs are not interacting with chemicals (nutrients), CheA and CheY are active, and the flagellum switches rotation to make the cell go in a different direction. Hopefully for the cell, the new direction it is traveling will have more nutrients that will interact with the MCPs and block more changes in direction by CheA/CheY activity.

You might ask, if chemical compounds are always bound to the MCPs, what if the cell begins going to passed the best environment and needs to turn around? Good question. That is where the other protein activated by CheA comes in, CheB. What makes this system unique is the ability to adapt to current conditions (nutrient chemical levels) so the cell can respond to new information. A set of protein enzymes act upon part of the MCPs that can cause a change in how rotated (think door knob again) the MCP is. If the MCP is always interacting with a nutrient, a protein called CheR changes the MCP structure and causes rotation back towards the non-interacting form of the MCP. When CheA is active, it can activate CheB which reverses the changes caused by CheR. Ultimately, the whole system remains sensitive to new information over a wide range of nutrient concentrations (a 1000-fold range).

This whole system and its parts and regulation took several years for me to understand. I’m sure I did not do it justice, but hopefully you can get a small glimpse into the truth about “simple” bacteria.

The path bacterial cells swim tracked using motion tracking software

One of the most prevalent ways a bacterium decides this is by using a two component system, or TCS. TCSs are relatively simple compared to chemotaxis. As you would suspect from the name, TCSs are pathways consisting of only two protein members, the sensor histidine kinase and the response regulator. Histidine kinases are a major protein family in bacteria because they are able to sense many different factors in the bacterium’s environment including nutrients, toxins, fellow bacteria, etc. In case you are wondering, chemotaxis is a modified form of a TCS in which the histidine kinase CheA is regulated by the activity of a separate protein, the methyl-accepting chemotaxis protein.

What if you are a bacterium and you have been using a certain type of carbon source to generate energy and suddenly that carbon source isn’t as prevalent? In this case, you would want to shut down the enzyme factories that were converting the previous food source into energy and begin preparing new enzyme factories to convert other food sources into energy as you prepare for starvation. If these conditions persist, you might want to decide to hibernate in the form of a spore or cyst until conditions around you improve. Or, if other food sources are sensed in the environment, any special enzymes that would be needed to convert them into energy would need to be synthesized from their respective genes. All of these scenarios are controlled by TCSs. The conditions are used as input for the cell to decide the best strategy to survive and thrive. Histidine kinase activation leads to a hand-off event from the kinase to the response regulator of a molecule which acts as a green light for the response regulator to proceed with its job. This job may be to turn on gene expression to produce proteins needed in the cell. The response regulator’s job may be to shut down gene expression for proteins no longer needed by the cell. It is a carefully orchestrated balancing act evolved over millions of years to make sure only the proteins/enzymes needed by the cell at a given time are present assuring highly valuable energy molecules are not wasted.

Getting the message

Second messengers are common from bacteria to humans. The major second messenger we all learn about in biochemistry class is cyclic AMP (cAMP). However, bacteria use several nucleotides as second messengers. Many are used as determinants in the decision making process, but one of the most recently discovered (and personal favorite) is cyclic-di-GMP, or c-di-GMP.

Bacteria are constantly processing signals both inside and outside their cell membranes. Hard to believe that one of the most abundant response molecules was only discovered in the late 1980s while researching how a certain species, Acetobacter xylinum now known as Gluconacetobacter xylinus, produced cellulose. Almost by accident, the Benziman lab discovered the enzyme responsible for cellulose production (cellulose synthase) was regulated by a nucleotide, later found to be c-di-GMP. Since that discovery, c-di-GMP has become a hot topic among microbiologists and immunologists due to the decisions bacteria make as the level of c-di-GMP increases within the cell. As I learned it, the concentration of c-di-GMP had predictable outcomes on the decisions of bacteria: high levels leads to loss of motility, increase in biofilm formation, changes in cell morphology, and increase in cell-cell communication. When low levels of c-di-GMP are present, the cell decides to move around (motility), become resistant to heavy metals, and, most importantly, becomes virulent. For example, Vibrio cholerae, the bad guy responsible for cholera, only decides to move around and produce cholera toxin when c-di-GMP levels are low in the cell. If levels increase, V. choleraewill produce biofilms via extracellular polysaccharide (EPS) production.

You might be asking yourself what controls the c-di-GMP levels of a bacterial cell. The initial discovery in the Benziman lab also found the enzymes/proteins that were responsible for making and breaking the second messenger. The long (and short) names are; for making c-di-GMP from 2 GTP molecules, diguanylate cyclases (DGCs aka GGDEF proteins) and degradation by phosphodiesterases (PDEs aka EAL proteins). GGDEF and EAL proteins are so called due to important amino acids necessary for their functions, GGDEF is glycine, glycine, aspartate, glutamate, phenylalanine, and EAL is glutamate, alanine, leucine. These enzymatic activities are usually controlled by regulatory protein domains common in bacteria (and humans). Signals from the environment (internal or external) can trigger changes in enzyme activity of GGDEFs and EALs thus changing the cellular concentration of c-di-GMP. This mechanism is well understood after 30 years of research. However, what happens next is still essentially unknown.

Cyclic-di-GMP levels rise within a bacterial cell. Now what? It was known early on that c-di-GMP itself could then interact with GGDEFs to inhibit activity. But what other proteins interact with c-di-GMP and help these bacteria decide to make major lifestyle changes? It wasn’t until 2006 that bioinformaticians predicted c-di-GMP binding to a protein, or protein domain. PilZ, an obscure protein of unknown function but necessary for Type IV pilimotility, was hypothesized to bind c-di-GMP. By the end of 2007, this prediction was verified and PilZ domain proteins were the first shown linking c-di-GMP to downstream proteins in pathways, or circus rings.

Transitioning from a free swimming/moving cell to life in a biofilm community is a major lifestyle change for bacteria. This decision takes commitment which is initiated by a small molecule.

Mystery of a mysterious kind

The decisions bacteria make weigh heavily on the amount of this molecule found within the cell. However, how a bacterial cell knows how much c-di-GMP there is ultimately remains a mystery. The focus of early research involved finding what regulated the synthesis and degradation of c-di-GMP. Thus, the majority of publications in print focus on the enzymes that perform these functions, GGDEFs and EALs. Also, by deleting certain GGDEFs or EALs from a bacterium, scientists were able to determine what effect this change would have on the cell’s decision making and lifestyle. Most research was performed in medically relevant species like Vibrio and Pseudomonas. This short-sighted focus has led to a distinct role of c-di-GMP in the cell that may not be absolute. I digress…

A cell produces c-di-GMP in response to some environmental signal. Now what?

Great question; one that is still not answered. Various proteins have been shown to interact with or bind c-di-GMP including the PilZ domain. The list of c-di-GMP effectors has grown slightly over the past few years to include examples of transcriptional regulators in both Vibrio and Pseudomonas (VpsT and FleQ, respectively). Transcriptional regulators are proteins that help carry out the decisions made by a cell by regulating gene transcription. However, these are only two examples from two bacteria. What about the vast number of other bacteria out there? How do they “see” c-di-GMP? Cyclic-di-GMP is a vital component to bacterial decision making even though our knowledge of how it is seen by a cell is a huge unknown.

My hypotheses and speculations (with some evidence)

In the last chapter of my dissertation (under embargo), I investigated what other protein domains could potentially bind c-di-GMP bioinformatically. Using my methods, I could predict proteins in the nonredundant database that could potentially bind c-di-GMP. One group of proteins I found were those already shown to bind other nucleotides like ATP. I was able to test my method against a publication that biochemistry and proteomics to identify c-di-GMP binding proteins from Pseudomonas. This crude “chemical proteomic” approach identified around 200 potential binding proteins of which the method I created also found several of the same proteins without the exhaustive time and effort of “wet bench” experiments.

This is not a post about how good I am at science. This is a post about using new and different methods to answer questions within science not unlike the investigation that identified the PilZ domain as the c-di-GMP binding protein in the first place. Unfortunately, my time in the lab was over before I could test my hypotheses, but my curiosity and passion live on. I will say that I predict receiver domains are very common c-di-GMP binding effectors that will be the next major discovery in this elusive mystery of how cells use c-di-GMP to make decisions.

It takes a village

The marvels of single celled organisms is that they are able to integrate all kinds of stimuli and make one grand decision that affects how they proceed. Bacteria do in one cell what we as humans do with billions. However, do bacteria contain the ability to think as a group or community?

The answer is absolutely. It is called quorum sensing. The pioneer for this research is Bonnie Bassler from Princeton University. Listening to her tell her story of the curiosity she felt when observing how and why a certain group of bacteria emitted light, or bio-luminescence is great. (Watch here). Through her investigation with a insignificant bacterium, Vibrio harveyi, she opened up a whole new field of microbiology.

Many bacteria synthesize signaling molecules that serve as messages to other bacteria saying, “I am here”. Since bacteria don’t have senses that we are familiar with like sight and hearing, these signaling molecules tell other bacteria who is around. When there aren’t a lot of bacteria sending out the signal, no big decisions are made. However, when enough bacteria are around to tell all other village members the approximate population, all village members act together to make a committed decision. In the case of V. harveyiit is the production of a light emitting molecule, but for other bacterial species it may be activation of pathogenicity. From the perspective of the bacterium, you don’t want to decide alone to make a big commitment like invading another organism. By taking a bacterial census through quorum sensing, these bacteria make a educated decision only when their population is high enough to make an impact. For some species, this critical number may be less than ten. However, in some cases, the population needs to be in the millions.

I think bacteria can teach us a very important lesson via quorum sensing: don’t go it alone. It takes a village.

How Old Are You?


My 4 year old daughter could tell you how old she is even though her concept of time is essentially nonexistent. She can’t wait to be “big”, which in her mind is 5 years old. However, the rest of us are not much better at answering the question about how old we are. Yes, we are correct about our legally recognized age, but we are way off on our natural age.

We’re all the same age…really old

Atomic level

Since everything is made up of matter, we all consist of atoms. These atoms all come together to make us who we are, but my daughters atoms are not 4 years old or even 4 billion years old. At some point shortly after the big bang, atoms came together thus forming the different elements (think periodic chart). Here we are 13.7 billion years later; all of us made of the same elements. This makes me shake my head when I think of nations going to war. We’re all made of the same elements, same matter. It doesn’t seem natural. With this argument, we are all really old at about 13.7 billion years old.

We’re all about the same age…really young

Cellular level

Humans consist of around 10 trillion human cells (excluding the 100 trillion microbial cells). These cells have a turnover rate that suggests each human consists of entirely different cells every 7 years. With this argument, we are all pretty young with no one older than 7 years old.

We’re all rentals…really short-lived
Since we’re all made up of the same atoms and these atoms have essentially been around forever, they have been used by other matter before us. And, most certainly, they will be used by matter long after we as humans are gone. Mother Nature sees us as atomic renters, but definitely not rent-to-own.

We’re all tenants…really big compared to our landlords
Something else I have been thinking about for a while now; almost everything we see or touch is completely covered with a thin layer of life, i.e. bacteria. They cover us. They cover our loved ones. They cover our…everything! Also, they have been around a lot longer than we have as species. We are just using the same space they are. Heck, we are a space they live! So, in this sense, they are allowing us to use this space as tenants. They are very nice landlords, too. Consider all the benefits we receive from their generosity (think microbiome).

Wanted: A Nation of Bill Nyes. Making science mainstream, fun, and relevant again

The United States rose to superpower status through a necessary, aggressive push towards innovation and scientific discovery in the last century. Many of the technologies developed in the last one hundred years were products of research funding by the U.S. government. In the old days, the gap between discovery/invention (public sector) and product development (private sector) was more easily traversed and companies were more than willing to take that leap. What scientists and engineers viewed was almost certainly drastically different from what consumers viewed, but either way, it was progress.

The world is a much different place now. Research funding (minus stimulus funding) has remained stagnant and the outlook is bleak.

One of the overlooked aspects of this funding is the community outreach and broader impacts that result from grants. This includes money for paying undergraduates and graduate students for research conducted in the grantee’s lab. From personal experience, most of the undergraduates that came through our lab when I was a graduate student were STEM majors. However, this is misleading because the goal after receiving their B.S. was to attend a professional school including medical, dental, and pharmacy schools. To date, only one out of twenty or so undergraduates from our lab later attended a STEM graduate program.

Why aren’t more students interested in STEM?

“A society’s competitive advantage will come not from how well its schools teach the multiplication and periodic table, but from how well they stimulate imagination and creativity”

-Albert Einstein, 1953

“Bear in mind that the wonderful things you learn in your schools are the work of many generations, produced by enthusiastic effort and infinite labor in every country of the world. All this is put into your hands as your inheritance in order that you may receive it, honor it, add to it, and one day faithfully hand it to your children.”

-Albert Einstein, 1934

Many professions have had their icons and role models. Einstein is arguably the most famous scientist to walk this planet. When once asked what was the best advice he could give to people, he said to always remember to put the shower curtain inside the tub before turning on the water. He had a sense of humor that made him relatable to the masses even though he saw the wonders of Nature as math equations. Einstein wrote a lot about curiosity, imagination, and enthusiasm. These qualities can be used in many ventures, but he chose Physics.


Bill Nye has never been accused of lacking enthusiasm. Having a genuine curiosity of how things work led to a degree in mechanical engineering. Most of us, however, know him as the Science Guy on TV. Spanning 100 episodes, Bill Nye the Science Guy laid a foundation for many across the country to explore curiosity and imagination. Nye took on current, relevant topics and made them relatable and understandable for children (and their parents).

For me, these shows were a time for exploration (virtually). I was able to better comprehend myself, nature, space, chemistry, etc. Times have changed and most people receive information from a variety of sources, some much more interactive. The technology to inspire children to pursue STEM careers are out there. However, where are the enthusiastic STEM crusaders and icons? Unfortunately, it’s not the teachers. They are too busy teaching mandated facts in a race to get through all the course material before the standardized tests in the spring…

As many have noted, the number of students who pursue a career in a STEM field fall well short of the demand from industry and see this as the problem. On the other hand, I see this as the result of the problem. At some point between toddler years and middle school, the inherent curiosity of a child fizzles; overtaken by media and gadgets. Have a question? Look it up on the Google app (I’m not criticizing Google. It is the best tool for any scientist). We, and our children, are constantly connected to everything going on in the world. For some it is politics or business, but for our children, it is Justin Bieber and Taylor Swift. To me, again, this is not the problem.

Let’s take a couple of other celebrities as examples: Brad Pitt and Will.i.am. We all know Pitt as an actor, however, we know him just as well for his charity work through the Jolie-Pitt Foundation. Will.i.am is a musician but is also into science as seen through his support for FIRST (For Inspiration and Recognition of Science and Technology) and its robotics competition. These are two examples of celebrities using their fame for a greater good.

STEM has an image problem in the United States. (A great survey sponsored by Microsoft showing the perception of STEM by students and parents can be found here). According to a study by Lenovo, the second leading hesitation to a career in STEM for U.S. students is that it requires too much work or school. The number one reason being that the student doesn’t feel confident in their ability. Here is the disconnect…if the passion and curiosity of the world around you and how to make it better is not there or hasn’t been curated, a STEM career is considered too much work. My Ph.D. took 6 and a half years to complete. I never once considered giving up or considered it too hard or too much work. To me, it wasn’t work. I felt lucky to be able to do what I loved and get paid for it.

In my humble opinion, keeping a child’s curiosity and imagination alive is a major step towards having real progress in attitudes and participation in STEM education. I personally wanted to be a doctor growing up. I was fascinated with how all cell types worked together. The checks and balances. As I grew older, in came the question of what specialty to go into as a medical professional. Knowing my interests, it seemed no ‘specialty’ was specialized enough. Then while working at a summer internship at the Oak Ridge National Laboratory, I went into an office with the Biochemical Pathways wall poster.

I could not take my eyes off of this masterpiece. To me, this poster symbolized life at the smallest scale but yet so sophisticated and precise; not to mention the signal transduction pathways that mediate the pathways output at any given time. I had found my calling. This visualization of what I had been taught in biology classes at all levels and biochem classes in college came to fruition.

For others, I’m sure it is different and I’m sure it’s not for everyone. The goal, inspire as many as possible to explore their curiosity of how life works and how they could make it better. Now the question, how do we do it?

Wanted: A Nation of Bill Nyes. Making science mainstream, fun, and relevant. Part 1.

The United States rose to superpower status through a necessary, aggressive push towards innovation and scientific discovery in the last century. Many of the technologies developed in the last one hundred years were products of research funding by the U.S. government. In the old days, the gap between discovery/invention (public sector) and product development (private sector) was more easily traversed and companies were more than willing to take that leap. What scientists and engineers viewed was almost certainly drastically different from what consumers viewed, but either way, it was progress.

The world is a much different place now. Research funding (minus stimulus funding) has remained stagnant and the outlook is bleak.

Screen Shot 2012-12-13 at 1.40.19 PM.png

One of the overlooked aspects of this funding is the community outreach and broader impacts that result from grants. This includes money for paying undergraduates and graduate students for research conducted in the grantee’s lab. From personal experience, most of the undergraduates that came through our lab when I was a graduate student were STEM majors. However, this is misleading because the goal after receiving their B.S. was to attend a professional school including medical, dental, and pharmacy schools. To date, only one out of twenty or so undergraduates from our lab later attended a STEM graduate program.

Why aren’t more students interested in STEM?

“A society’s competitive advantage will come not from how well its schools teach the multiplication and periodic table, but from how well they stimulate imagination and creativity”

Albert Einstein, 1953