Statistical analysis and molecular dynamics simulations of ambivalent α-helices.

ABSTRACT:

Background

Analysis of known protein structures reveals that identical sequence fragments in proteins can adopt different secondary structure conformations. The extent of this conformational diversity is influenced by various factors like the intrinsic sequence propensity, sequence context and other environmental factors such as pH, site directed mutations or alteration of the binding ligands. Understanding the mechanism by which the environment affects the structural ambivalence of these peptides has potential implications for protein design and reliable local structure prediction algorithms. Identification of the structurally ambivalent sequence fragments and determining the rules which dictate their conformational preferences play an important role in understanding the conformat

SUBMITTER: Bhattacharjee N 

PROVIDER: S-EPMC2973962 | biostudies-literature | 2010 Oct

REPOSITORIES: biostudies-literature