casein

Case number:845799-985836
Topic:Biochem
Opened by:phoagy
Status:Closed
Type:Suggestion
Opened on:Sunday, March 22, 2009 - 02:54
Last modified:Friday, January 6, 2012 - 21:44

Can you set up phosphoserine peptides that might help in modeling casein, a protein that does not want to fold into minimized crystalizable structures that can be crystallized? The phosphoserine residue by itself is restrained by a weak hydrogen bond between the gamma O and the alpha NH of the PSE (personal observation). The phosphate O's disrupt downstream backbone H-bonds. In addition, internal salt bridges with Lys or Arg are possible strong interactions. I am a retired chemist who did limited molecular modeling of some casein components and model phoshopetides. Your fold.it program is great! I like the way you have restricted the movement of side chains to reasonable angles.

(Sun, 03/22/2009 - 02:54  |  2 comments)


admin's picture
User offline. Last seen 3 weeks 5 days ago. Offline
Joined: 11/10/2007
Groups: vi users

Assigning to a biochemist.

spmm's picture
User offline. Last seen 36 weeks 2 days ago. Offline
Joined: 08/05/2010
Groups: Void Crushers
Status: Open » Closed

closed, resolved, implemented or no votes, comments since 2009

Sitemap

Developed by: UW Center for Game Science, UW Institute for Protein Design, Northeastern University, Vanderbilt University Meiler Lab, UC Davis
Supported by: DARPA, NSF, NIH, HHMI, Amazon, Microsoft, Adobe, RosettaCommons