BIOL 185 |
| α-crystallin is the major structural protein in the mammalian lens. The tertiary and quaternary structures of α-crystallin are still unknown because of the difficulties in successful crystallization. Computational studies on the interactions between the two subunits can contribute to our understanding of how aggregation of α-crystallin occurs and suggest possible models of the quaternary structure of α-crystallin aggregates. The sequences of the subunits are obtained from the SWISSPROT database. The models for the subunits are built up by a fold recognition method and optimized by molecular mechanics methods. A docking program is used to build up the models for α-crystallin dimers according to the surface complementary principal. A molecular dynamics method is used to simulate the approach and attainment of equilibrium for the dimers and to study the interactions. The simulation results indicate hydrogen bonds play very important roles in the formations of dimers. |
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Frontiers in Chemical Biology
5:00 PM-7:00 PM, Wednesday, August 22, 2007 BCEC -- Exhibit Hall - B2, Poster
Division of Biological Chemistry |