Use of 13C(alpha) chemical shifts for accurate determination of beta-sheet structures in solution.

ABSTRACT: A physics-based method, aimed at determining protein structures by using NOE-derived distance constraints together with observed and computed 13C(alpha) chemical shifts, is applied to determine the structure of a 20-residue all-beta peptide (BS2). The approach makes use of 13C(alpha) chemical shifts, computed at the density functional level of theory, to derive backbone and side-chain torsional constraints for all of the amino acid residues, without making use of information about residue occupancy in any region of the Ramachandran map. In addition, the torsional constraints are derived dynamically--i.e., they are redefined at each step of the algorithm. It is shown that, starting from randomly generated conformations, the final protein models are more accurate than existing NMR-derived mo

SUBMITTER: Vila JA 

PROVIDER: S-EPMC2542864 | biostudies-literature | 2008 Feb

REPOSITORIES: biostudies-literature