My PhD is in macromolecular and structural biochemistry. More specifically I study the dynamics of proteins using X-ray crystallography. Before I can start any conversation about my research, I first ask, "do you know what a protein is?" It helps me gauge the level of understanding of the person I'm conversing with.
The central dogma of biochemistry is... DNA -> mRNA -> Protein.
Most people know DNA as the language that encodes genetic information. The instructions for each gene are transcribed into messenger RNA (mRNA), and a small organelle called the ribosome translates the RNA message into protein.
Humans have roughly 19,000 distinct genes. One gene often encodes multiple splice variations, so humans are estimated to have 30,000 - 35,000 different expressed proteins, and each one has a different role to perform within the cell.
The concentration of protein in a typical cell is 200 g/l, which is roughly 20% of the cell volume, and water fluctuates between 70-80%. This means the majority of the cellular milieu is protein. It is pretty amazing how all the proteins in the cell are able to communicate synchronously with each other despite all the traffic http://www.mcponline.org/content/13/12/3497.full
http://iopscience.iop.org/article/10.1088/1478-3975/2/2/S01/fulltext/
Proteins are a polymer of amino acids. The sequence of amino acids is called the primary structure. If you could imagine, each amino acid is a link a chain. Although the length of these chains can vary from 2 to 3000+ amino acids, a protein is typically considered longer than 50 amino acids. Aspartame is actually a dimer of two amino acids (aspartate and phenylalanine).
Each of the 20 amino acids have different physical characteristics, which causes the chain of amino acids to adopt a canonical structure, called the secondary structure (depicted as helices and arrows in the image below). The structure of a protein determines its function, and the structure is evolutionarily conserved. Mutations that affect a protein's structure are often the basis for prevalent diseases and disorders. For example, sickle cell anemia is cause by replacing one link the amino acid chain of hemoglobin. https://evolution.berkeley.edu/evolibrary/article/mutations_06
this is a model of the caspase-6 protein (made with X-ray crystallography), and only shows the secondary and tertiary structure.
So, when we eat "protein" we are essentially recycling the amino acids from an external source, so that we can re-use the amino acid building blocks for our own cells.
The take home point is that "protein" does not translate to "meat."
-The Scientist
As a toxicologist, I only deal with proteins at the functional level. Nice to see the chemical basics behind it repeated.
Edit: @OriginalWorks
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The @OriginalWorks bot has determined this post by @thescientist to be original material and upvoted it!
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Thank you for your post @thescientist! I study chemistry and biochemistry right now! This threw me right back into my biochemistry introductory class haha!
What is your PhD work focused on?
Cheers!
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I use evolutionary biology to reconstruct the evolutionary path of caspase proteins. I want to understand how discrete regulatory mechanisms evolved among the 12 human caspases, so that we can potentially manipulate them with rationally designed drugs.
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Got ya! So you compare the structures of caspases with Xray crystallography and then try to find substrate analogues with high throughput screening?
I am following you now! It would be cool if you would maybe look at my blog also. I am not asking for upvotes or you following me, just suggestions and ideas!
Cheers!
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followed. I compare the amino acid sequences of all caspases, including rat, bat, cat, ect... and then predict the sequence of the common ancestor. Then I resurrect the ancestral gene and crystallize it
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That is very cool! Chemistry is so fascinating. I may end up going into the development of new instruments. Anyways, good luck! Cheers!
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