Quantum chemical 13C(alpha) chemical shift calculations for protein NMR structure determination, refinement, and validation.

ABSTRACT: A recently determined set of 20 NMR-derived conformations of a 48-residue all-alpha-helical protein, (PDB ID code 2JVD), is validated here by comparing the observed (13)C(alpha) chemical shifts with those computed at the density functional level of theory. In addition, a recently introduced physics-based method, aimed at determining protein structures by using NOE-derived distance constraints together with observed and computed (13)C(alpha) chemical shifts, was applied to determine a new set of 10 conformations, (Set-bt), as a blind test for the same protein. A cross-validation of these two sets of conformations in terms of the agreement between computed and observed (13)C(alpha) chemical shifts, several stereochemical quality factors, and some NMR quality assessment scores reveals the goo

SUBMITTER: Vila JA 

PROVIDER: S-EPMC2567219 | biostudies-literature | 2008 Sep

REPOSITORIES: biostudies-literature