Simultaneous assignment and structure determination of a membrane protein from NMR orientational restraints.

ABSTRACT: A solid-state NMR approach for simultaneous resonance assignment and three-dimensional structure determination of a membrane protein in lipid bilayers is described. The approach is based on the scattering, hence the descriptor "shotgun," of (15)N-labeled amino acids throughout the protein sequence (and the resulting NMR spectra). The samples are obtained by protein expression in bacteria grown on media in which one type of amino acid is labeled and the others are not. Shotgun NMR short-circuits the laborious and time-consuming process of obtaining complete sequential assignments prior to the calculation of a protein structure from the NMR data by taking advantage of the orientational information inherent to the spectra of aligned proteins. As a result, it is possible to simultaneously assi

SUBMITTER: Marassi FM 

PROVIDER: S-EPMC2312444 | biostudies-literature | 2003 Mar

REPOSITORIES: biostudies-literature