Protein structure validation and identification from unassigned residual dipolar coupling data using 2D-PDPA.

ABSTRACT: More than 90% of protein structures submitted to the PDB each year are homologous to some previously characterized protein structure. The extensive resources that are required for structural characterization of proteins can be justified for the 10% of the novel structures, but not for the remaining 90%. This report presents the 2D-PDPA method, which utilizes unassigned residual dipolar coupling in order to address the economics of structure determination of routine proteins by reducing the data acquisition and processing time. 2D-PDPA has been demonstrated to successfully identify the correct structure of an array of proteins that range from 46 to 445 residues in size from a library of 619 decoy structures by using unassigned simulated RDC data. When using experimental data, 2D-PDPA succes

SUBMITTER: Fahim A 

PROVIDER: S-EPMC4090686 | biostudies-literature | 2013 Aug

REPOSITORIES: biostudies-literature