Cysteines

Things like Cu, Pb, and Hg bind strongly to the sulfurs of cysteines. They can sometimes bind to Histidines or the sidechains of Aspartates and Glutamates. They will sometimes displace structurally important metals, but the heavy metals are large (relative ...

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Anfinsen used the protein RNase A (has a single polypeptide chain with 8 cysteines). Anfinsen wanted to know if there are substances within cells (enzymes?) that cause other proteins to fold properly into their appropriate 3D shapes. His first step was to apply ...

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... never thought that the ultimate sequence of the peptide dictated the choice of resin, unless it has something to do with “difficult” residues like cysteines or methionines, for example—but then, I’m not a peptide chemist, either. EMDNovabiochem (one of many potential sources) sells t-BOC and fMOC ...

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... but what I found perusing PubMed: SNAP = soluble NSF attachment protein(s?) NSF = N-ethylmaleimide sensitive factor (N-ethylmaleimide reacts with cysteines) SNARE = SNAP Receptor They seem to be involved in membrane fusion processes and so could be involved in any number of things including, but ...

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Well off the top of my head I would say that the amino acids involved would be two cysteines. I dont know of another a.a. that creates di-sulfide bonds? but I am no chemist.

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