Determination of protein backbone structures from residual dipolar couplings.

ABSTRACT: There are a number of circumstances in which a focus on determination of the backbone structure of a protein, as opposed to a complete all-atom structure, may be appropriate. This is particularly the case for structures determined as a part of a structural genomics initiative in which computational modeling of many sequentially related structures from the backbone of a single family representative is anticipated. It is, however, also the case when the backbone may be a stepping-stone to more targeted studies of ligand interaction or protein-protein interaction. Here an NMR protocol is described that can produce a backbone structure of a protein without the need for extensive experiments directed at side chain resonance assignment or the collection of structural information on side chains.

SUBMITTER: Prestegard JH 

PROVIDER: S-EPMC1808351 | biostudies-literature | 2005

REPOSITORIES: biostudies-literature