Backbone resonance assignment and order tensor estimation using residual dipolar couplings.

ABSTRACT: An NMR investigation of proteins with known X-ray structures is of interest in a number of endeavors. Performing these studies through nuclear magnetic resonance (NMR) requires the costly step of resonance assignment. The prevalent assignment strategy does not make use of existing structural information and requires uniform isotope labeling. Here we present a rapid and cost-effective method of assigning NMR data to an existing structure-either an X-ray or computationally modeled structure. The presented method, Exhaustively Permuted Assignment of RDCs (EPAR), utilizes unassigned residual dipolar coupling (RDC) data that can easily be obtained by NMR spectroscopy. The algorithm uses only the backbone N-H RDCs from multiple alignment media along with the amino acid type of the RDCs. It is in

SUBMITTER: Shealy P 

PROVIDER: S-EPMC4071608 | biostudies-literature | 2011 Aug

REPOSITORIES: biostudies-literature