Protein loop closure using orientational restraints from NMR data.

ABSTRACT: Protein loops often play important roles in biological functions. Modeling loops accurately is crucial to determining the functional specificity of a protein. Despite the recent progress in loop prediction approaches, which led to a number of algorithms over the past decade, few rigorous algorithmic approaches exist to model protein loops using global orientational restraints, such as those obtained from residual dipolar coupling (RDC) data in solution nuclear magnetic resonance (NMR) spectroscopy. In this article, we present a novel, sparse data, RDC-based algorithm, which exploits the mathematical interplay between RDC-derived sphero-conics and protein kinematics, and formulates the loop structure determination problem as a system of low-degree polynomial equations that can be solved exa

SUBMITTER: Tripathy C 

PROVIDER: S-EPMC3305838 | biostudies-literature | 2012 Feb

REPOSITORIES: biostudies-literature