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<StructureSection load='2AGG' size='340' side='right' caption='Trypsin Mechanism' scene=''> | <StructureSection load='2AGG' size='340' side='right' caption='Trypsin Mechanism' scene=''> | ||
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. '''Sandbox wabash23'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | 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. '''Sandbox wabash23'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | ||
| - | You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID: | + | You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:16636277</ref> to the rescue. |
== Function == | == Function == | ||
Revision as of 16:49, 12 February 2016
The Mechanism of Trypsin
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References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Radisky ES, Lee JM, Lu CJ, Koshland DE Jr. Insights into the serine protease mechanism from atomic resolution structures of trypsin reaction intermediates. Proc Natl Acad Sci U S A. 2006 May 2;103(18):6835-40. Epub 2006 Apr 24. PMID:16636277
