CHED 237 |
| Studies show that cells can use intracellular pH to regulate actin-based motility. At a molecular level we discovered a correlation between pH changes and the structure of talin, an actin binding protein. Computational methods were used to investigate a homology model of the C terminal region in the I/LWEQ domain of the structure HIP1R. In the five helices, five side chains were predicted to have pKa's near a physiological pH. A histidine and four aspartic or glutamic acids with strongly shifted pKa's were all clustered at one end. Constant-pH molecular dynamic simulations revealed protonation states between pH 6 and 7.5 and the protein's conformational changes, allowing the residues to functions as pH sensors. In correlation with experimental results, at a higher pH the first helix, otherwise known as the USH, traveled away from the other helices, exposing a “cryptic” binding site. |
|
Undergraduate Research Poster Session: Chemical Education
2:30 PM-4:30 PM, Monday, 11 September 2006 Moscone Center -- Hall D, Poster
Division of Chemical Education |