Trypsin works to cleave peptide chains at the carboxyl site of amino acids. Its role is to hydrolyze proteins. More specifically, trypsin uses the histidine residue as a base to activate serine protease making it a better nucleophile. The histidine then acts as an acid which donates the proton from the nitrogen to the peptide leaving group. This information came from the paper by Radisky,Evette S., Lee, Justin M., Karen Lu, Chia-Jung and Koshland, Jr. Daniel E.You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue.
Function
Disease
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Structural highlights
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