I don't have my notebook on me but someone who was on The Proteomics Show dropped a knowledge bomb on us about cysteines a couple of years ago. She said something like only 12% of cysteines are involved in those disulfide bridges we're all so worried about. Might have been a he and might have been 2 or 40%.
So...when this PI is in the lab, he commonly skips the alkylation and reduction steps. Not just because he doesn't know where the reagents are, but also because I spent a couple of years studying drugs that bind cysteines. True story, about 1/4 of the pharmacology faculty at Pitt seem to study similar drugs.
This group shows that it might be a good idea even beyond cysteine alkylating compounds!
For real, what are all those other cysteines doing? Just being sulfury? Sulfur isn't the most abundant thing and it only gets incorporated as a nutrient by plants through a painstaking process that starts with a slow oxidation by bacteria. Seems like a lot of work for something that just does a couple of things, right? Evolution is too cheap for many single use materials.
Super cool paper and definitely worth thinking about when you can't find that DTT thing on your first pass through the -20C? Chemical cabinet? I honestly don't know.
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