Protein Heteronuclear NMR Assignments Using Mean-Field Simulated Annealing

• Published in: Journal of magnetic resonance (1997) Vol. 125; no. 1; pp. 34 - 42
• Main Authors: Buchler, Nicolas E.G, Zuiderweg, Erik R.P, Wang, Hong, Goldstein, Richard A
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.03.1997
• Subjects: Computer Simulation; Magnetic Resonance Spectroscopy - methods; Molecular Weight; Proteins - chemistry
• ISSN: 1090-7807; 1096-0856
• DOI: 10.1006/jmre.1997.1106

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 HNCα, HN(CO)Cα, HN(Cα)Hα, and Hα(CαCO)NH and spin-system identification data obtained from CP-(H)CCH–TOCSY and CP-(H)C(CαCO)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 theE. coliheat-shock protein, DnaK. The method is demonstrated to be robust to significant amounts of missing, spurious, noisy, extraneous, and erroneous data.