BIOL 68 |
| β-sheets are a common secondary structural element observed in polypeptides and proteins. Because of force field bias towards α-helices, β-sheets were challenging to simulate until recently. We propose that two recent molecular dynamics protocols developed within our group can help to determine low energy conformations based entirely upon primary sequence. We search for conformations near absolute zero temperature, which gives us low potential energy conformations, and also near in vivo temperatures, based upon our findings from the low potential energy conformations. Two structures were selected for study: tryptophan zipper 2 (trpzip2) and residues 41-56 of the B1 domain of protein G (peptide G). By using both protocols in conjunction, we are able to obtain conformations that are < 2.0 Å backbone RMSD in agreement with experimental structures. |
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Protein Structure and Folding
4:30 PM-6:30 PM, Sunday, 10 September 2006 Moscone Center -- Hall D, Poster
Sci-Mix
Division of Biological Chemistry |