Fine grained sampling of residue characteristics using molecular dynamics simulation.

Computational Biology and Chemistry
Hyun JooJerry Tsai

Abstract

In a fine-grained computational analysis of protein structure, we investigated the relationships between a residue's backbone conformations and its side-chain packing as well as conformations. To produce continuous distributions in high resolution, we ran molecular dynamics simulations over a set of protein folds (dynameome). In effect, the dynameome dataset samples not only the states well represented in the PDB but also the known states that are not well represented in the structural database. In our analysis, we characterized the mutual influence among the backbone phi,psi angles with the first side-chain torsion angles (chi(1)) and the volumes occupied by the side-chains. The dependencies of these relationships on side-chain environment and amino acids are further explored. We found that residue volumes exhibit dependency on backbone 2 degrees structure conformation: side-chains pack more densely in extended beta-sheet than in alpha-helical structures. As expected, residue volumes on the protein surface were larger than those in the interior. The first side-chain torsion angles are found to be dependent on the backbone conformations in agreement with previous studies, but the dynameome dataset provides higher resolution of ...Continue Reading

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Jan 10, 2012·Journal of Computational Chemistry·Sampath Koppole, Michael Schaefer

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