Protein Heteronuclear NMR Assignments Using Mean-Field Simulated Annealing
Authors: Buchler, N.E.G.; Zuiderweg, E.R.P.; Wang, H.; Goldstein, R.A.
Source: Journal of Magnetic Resonance, Volume 125, Number 1, March 1997 , pp. 34-42(9)
Publisher: Academic Press
Abstract:A computational method for the assignment of the NMR spectra of larger (21 kDa) proteins using a set of six of the most sensitive heteronuclear multidimensional nuclear magnetic resonance experiments is described. Connectivity data obtained from HNC alpha , HN(CO)C alpha , HN(C alpha )H alpha , and H alpha (C alpha CO)NH and spin-system identification data obtained from CP-(H)CCH-TOCSY and CP-(H)C(C alpha CO)NH-TOCSY were used to perform sequence-specific assignments using a mean-field formalism and simulated annealing. This mean-field method reports the resonance assignments in a probabilistic fashion, displaying the certainty of assignments in an unambiguous and quantitative manner. This technique was applied to the NMR data of the 172-residue peptide-binding domain of the E. coli heat-shock protein, DnaK. The method is demonstrated to be robust to significant amounts of missing, spurious, noisy, extraneous, and erroneous data.
Document Type: Research Article
Affiliations: Biophysics Research Division
Publication date: March 1, 1997