The Biochemical Society has a contest for undergrads to write a 1500 essay on a biomolecular topic targeted to a general audience. Though the deadline has passed for this year, it might be a good way of practicing scientific communication in the future!
There are some really great past winners at the bottom – I particularly liked “Epigenetics: The Bee’s Knees” but I may be a bit biased after spending so much time learning about nucleosomes for the past semester. 🙂
The serotonin transporter protein (SERT) is a monoamine transporter protein that is responsible for terminating serotonin binding and then recycling the compound. Transport of serotonin into the cell is driven by higher concentration of Na+ outside the cell, which is maintained by Na+/K+ pumps. One mechanism that antidepressant medications use is to reduce SERT activity so that there is more serotonin available to bind with serotonin receptors. One of the most common classes of antidepressants selective serotonin reuptake inhibitors (SSRIs) act by binding to SERT and reducing SERT’s affinity for serotonin (thus preventing its transported back into the neuron).
In general, anemia is a condition that occurs when a person’s blood lacks red blood cells or hemoglobin. The most common type of anemia is caused by iron deficiency, and can be treated with iron supplements. However, Thalassemia is a heritable form of anemia which caused by mutations in hemoglobin. Wild type hemoglobin consists of four different subunits, two alpha chains and two beta chains, which are each conjugated to a heme group. People with thalassemia anemia have mutations in the genes that code for alpha or beta chains, which results in malformed hemoglobin molecules with fewer heme groups. Depending on the number of nonfunctional genes, the oxygen capacity of red blood cells can be reduced to the point that the person cannot survive without regular blood transfusions.
In cell phys, we briefly talked about the biological importance of gap junctions, which are relatively small pores that connect adjacent cells. These junctions are important for biochemistry because it allows some small molecules and ions to passively diffuse from cell to cell. The gap junction complex is formed from two different connexon complexes, and both of the adjacent cells contain one of these complex which are lined up across from each other, spanning the extracellular space. The connexons are transmembrane proteins which are made up of six different identical subunits (which are themselves four-pass transmembrane proteins) that can rotate to open or close the pore. One of the most important biological uses for this is in neuronal cells, where membrane potential can quickly be passed from cell to cell as ions diffuse through the gap junctions.
In our presentation on Friday, we didn’t really have time to talk about the specifics of how dorsal ventral patterning occurs in Drosophila. The key protein in this pathway is a morphogen called Dorsal, which is responsible for activating the genes associated with ventral identity. Dorsal is found throughout a developing embryo, but it only enters the nucleus of ventral cells, indicating that something else is responsible for signaling Dorsal to enter the nucleus. The Spz-Toll complex comes into play because cleavage of Spz only occurs on the ventral side of the embryo (and thus Toll is only activated on the ventral side). Activation of Toll turns on a kinase which frees Dorsal from its chaperone protein and allows Dorsal to enter the nucleus.
This last week of presentations was not only extremely rewarding in the sense that it wrapped up nicely all the themes were were learning about this semester, but also because it was a great insight into the world of science education.
I’ve given a ton of presentations in my Wellesley career, but it’s not often than I have the presentation be to a lay audience — and so it was not just the material we had to prepare, but also how Houda, Becca, and I decided to convey the material, which probably took up the bulk of our planning. It’s these delicate details that can change everything– the small, subtle strategies, the organization of presentation, the decision of what words to emphasis and in what way, the improvisation one must convey when they realize the audience isn’t getting the message exactly as the presenters had hoped. It’s a delicate balance between delivering material that is too elementary and material that is too confounding, and an equally dizzying challenge trying to facilitateorganic aha! moments – human reaction is not so predictable as we’d think.
So this left me thinking about my own science education ever since elementary school and I am very lucky to say I’ve been gifted with many great science teachers. Even so, I don’t think I began to appreciate the connectivity of science (physics to chemistry, chemistry to biology, physical biochemistry, etc, etc – I used to make jokes about how ridiculous it was to have physical biochemistry and chemical biophysics as two distinct subjects because I didn’t understand why and how they differed!) until maybe two years ago. And maybe it’s just me, but it’s this feeling of being connected that is what helps these rather confusing science concepts stick. This realization that it’s not all pointless knowledge (physics, hem hem) but rather it is the reason our world exists as we know it. I think it’s too much to ask that every single student ace their physics exams, but if we can appreciate why it’s interesting, important, absolutely necessary, I feel like we’ll have a better chance of remembering the content.
I would also like to take the time to discuss the importance of science educators in the community – the translators who are equally fluent in science-speak and lay-people speak. Neil deGrasse Tyson (NdGT) is one person who comes to mind. and he is a bad-ASS (excuse my French!) !! Although I don’t really follow with his work as an astrophysicist, but I have seen him talk countless times on TV shows, panels, websites. And he has such an air about him that it’s really, really hard not to get inspired. He’s infectious, but not cheesy about it. An amazing person!
I wanted to pose this question to the class, in case someone might know — Who is the public face of biochemistry? I honestly don’t know but I wish I did, because if I had someone explain to me what it meant to meld biology and chemistry together, I might have jumped on the biochemistry track a little sooner! Again, it’s a little difficult to say all this without thinking through the logistics — biochem only really CLICKS when you’ve got the foundational chemical knowledge and the biological appreciation. All the same, I want a Neil for biochemistry because now I have 145 exciting and interesting biochemically-based stories for cocktail hour, thanks to this blog. Perhaps someone in our class will rise to the occassion 🙂
Lastly, I wanted to end with this video clip about women in science and what Neil deGrasse Tyson has to say about it. The good stuff starts at 1:01:28.
If you’ve clicked the stylized Google logo today you’ll be led to the page of Dorothy Hodgkin, who was a British biochemist is credited with the development of protein crystallography!
For the confirmation of the structure of Vitamin B12, she even was awarded a Nobel Prize, becoming only the 3rd woman to receive one! He moved the techniques of X-Ray crystallography forward, even deciphering the structure of insulin.
When she was 18, already with a passion for Chemistry, she entered Somerville College, Oxford, which was at the time on of the few women’s colleges. She even studied for a PhD at Cambridge. She was also one of the first to travel from Oxford to Cambridge in April 1953 to view Watson and Crick’s model based on Franklin’s research!
We’re finally getting some long awaited sun on this campus! This made me think about how vitamin D was discussed by the Lipid group on Wednesday (which by the way was a great presentation)! Again, this goes along with a major theme of the class that biochemistry is everywhere! Just a recap, vitamin D is produced by the body in response to sunlight and it also occurs naturally in a few foods, like fish and egg yolk, etc.
An interesting article that was published recently found that patients with lower vitamins D reported the highest pain level. This participants in this study were those who were in chronic pain and they noted their pain levels on a scale of 1-10 when a clamp was placed on a patients’ nail bed of the middle fingers. More studies still need to be conducted, but what could this possibly hint at for the future? Too much sunlight could potentially lead to more pain in a future accident? What would you do: to get vitamin D or not to?
Article for your reference: http://www.techtimes.com/articles/6743/20140509/vitamin-d-research-reveals-levels-may-impact-body-pain-threshold-study.htm
As the semester winds down and everybody gears up for finals, I’m starting to find a lot of exciting connections between all of my classes. It’s a pretty great feeling, and it always amazes me how exciting it is to be at a place in my academic career where I can start to synthesize all of the knowledge I’ve acquired. This week, I spent a lot of time thinking about computational chemistry and the technology involved in biochemical research. I’m currently enrolled in CS112, which is a computer science course for science majors that teaches Matlab. I’m no coding prodigy, but I really love how efficient and powerful the Matlab program is. Recently, I realized that PDB saves its files in PNG format, which is compatible with Matlab. I think this is super exciting, because I can now upload protein information directly into Matlab and create original programs using the data. I haven’t quite figured out what I’m going to do with this information, but after loading a few protein structures into Matlab and playing around with the files, I think I’m going to spend some time over the summer experimenting with designing programs for data analysis. In any case, I thought it would be nice to conclude this blogging experience in biochem with some thoughts about where I hope to go in the future with biochemistry. Thanks for a great year, and I hope your finals go well!
I also wanted to congratulate all of you for your wonderful presentations this past week. They were both biochemically sound and insightful and also extremely creative in a variety of ways. I couldn’t have asked for a better wrap up from you for the wonderful semester we had. I am REALLY very proud of seeing how far you have come along not only in your chosen field, but also as brilliant individuals.
I have also been enjoying your blogs immensely, and learning so much from them. It looks like many of you find it also as an enjoyable and effective way to share your experiences and thoughts. So let me remind you that you will definetely have this blogging site available for the rest of your wellesley time and I wanted to let you know that I am working with the IT to see if we can sort of make it permenant. So keep blogging over summer and keep your “networking” going. You can also give the website address to others who will be able to contribute, but it will go through an internal check to make sure that the context is not offensive.
Finally, after your presentations and Becca’s blog, you might also enjoy reading the blogs from the Art of Science seminar course.
https://blogs.wellesley.edu/chem106sp14/
Good luck with all your finals and remember Zoe’s tidbits of the three Cs…
