Assessing the accuracy of protein structures by quantum mechanical computations of 13C(alpha) chemical shifts.

ABSTRACT: Two major techniques have been used to determine the three-dimensional structures of proteins: X-ray diffraction and NMR spectroscopy. In particular, the validation of NMR-derived protein structures is one of the most challenging problems in NMR spectroscopy. Therefore, researchers have proposed a plethora of methods to determine the accuracy and reliability of protein structures. Despite these proposals, there is a growing need for more sophisticated, physics-based structure validation methods. This approach will enable us to (a) characterize the "quality" of the NMR-derived ensemble as a whole by a single parameter, (b) unambiguously identify flaws in the sequence at a residue level, and (c) provide precise information, such as sets of backbone and side-chain torsional angles, that we ca

SUBMITTER: Vila JA 

PROVIDER: S-EPMC3396562 | biostudies-literature | 2009 Oct

REPOSITORIES: biostudies-literature