title: Protein heteronuclear NMR assignments using mean-field simulated annealing.
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.
authors.affiliation: Biophysics Research Division, University of Michigan, Ann Arbor 48109-1055, USA.
authors.forename: N E
authors.initials: NE
authors.lastname: Buchler
authors.forename: E R
authors.initials: ER
authors.lastname: Zuiderweg
authors.forename: H
authors.initials: H
authors.lastname: Wang
authors.forename: R A
authors.initials: RA
authors.lastname: Goldstein
mesh_terms: D003198:Computer Simulation; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008970:Molecular Weight; D011506:Proteins / Q000737:chemistry*
chemical_list: D011506:Proteins