Assignment of proton, nitrogen-15, and backbone carbon-13 resonances in detergent-solubilized M13 coat protein via multinuclear multidimensional NMR: A model for the coat protein monomer

Autor:	Wymenga Ss, van de Ven Fj, M. L. Remerowski, Ruud N.H. Konings, C. W. Hilbers, van Os Jw, Aelen Jm
Rok vydání:	1993
Předmět:	NMR spectra database chemistry.chemical_compound Monomer chemistry Heteronuclear molecule Stereochemistry Nuclear magnetic resonance spectroscopy Sodium dodecyl sulfate Solubility Biochemistry Peptide sequence Micelle
Zdroj:	Biochemistry. 32:8322-8328
ISSN:	1520-4995 0006-2960
DOI:	10.1021/bi00083a036
Popis:	The major coat protein (gVIIIp) of bacteriophage M13 complexed with SDS detergent micelles was used as a model system to study the lipid-bound conformation of the protein. Conditions were found that allowed the recording of good quality of NMR spectra. By making extensive use of three-dimensional heteronuclear (13C, 15N) NMR, we obtained a complete set of resonance assignments for 1HN, 1H alpha, 1H beta, 13C alpha, CO, and 15N and partially assigned the rest of the 1H spectrum. Analysis of NOE and chemical shift data reveals that gVIIIp is composed of two alpha-helical domains, one ranging from Pro-6 to Glu20 and the other ranging from Tyr-24 all the way to the C-terminus Ser-50. In contrast to the results reported by Henry and Sykes [Henry, G.D., & Sykes, B.D. (1992) Biochemistry 31, 5285-5297], at a high SDS to protein ratio the protein appears to be monomeric.
Databáze:	OpenAIRE
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