Sandbox Reserved 835

This Sandbox is Reserved from Jan 1, through May 1, 2014 for use in a Biochemistry course taught by Ann Taylor at the University of Tennessee, Knoxville, USA. This reservation includes Sandbox Reserved 440 through Sandbox Reserved 450 and Sandbox Reserved 835 through Sandbox Reserved 894.

To get started:

Click the edit this page tab at the top. Save the page after each step, then edit it again.
Click the 3D button (when editing, above the wikitext box) to insert Jmol.
show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc.

More help: Help:Editing

Trypsin: an example of a serine proteaseTrypsin: an example of a serine protease

Trypsin is a serine protease that hydrolyzes peptides on the carboxyl side of hydrophobic residues. It works with a catalytic triad of aspartic acid, histidine and serine to catalyze the formation of a covalent intermediate with the substrate. This structure shows the binding of trypsin to a competitive inhibitor, leupeptin. There is a hydrophobic binding pocket to help align the substrate protein with the enzyme, and an oxyanion hole to stabilize the intermediate. Radisky ES, Lee JM, Lu CJ, Koshland DE Jr, Proc Natl Acad Sci U S A. 2006 May 2;103(18):6835-40. Epub 2006 Apr 24. PMID:16636277