PMID:1385726

Citation	Norwood, TJ, Crawford, DA, Steventon, ME, Driscoll, PC and Campbell, ID (1992) Heteronuclear 1H-15N nuclear magnetic resonance studies of the c subunit of the Escherichia coli F1F0 ATP synthase: assignment and secondary structure. Biochemistry 31:6285-90
Abstract	Nuclear magnetic resonance (NMR) studies of the c subunit of F1F0 ATP synthase from Escherichia coli are presented. A combination of homonuclear (1H-1H) and heteronuclear (1H-15N) 2D and 3D methods was applied to the 79-residue protein, dissolved in trifluoroethanol. Resonance assignment for all the backbone amide groups and many C alpha H side-chain protons was achieved. Analysis of inter- and intraresidue 1H-1H nuclear Overhauser effect (NOE) data and scalar coupling constant information indicates that this protein contains two extended regions of predominant alpha-helical character (residues 10-40 and 48-77) separated by an eight-residue segment which displays little evidence of ordered secondary structure. This model is consistent with information about the molecular motion of the protein deduced from 15N-1H heteronuclear NOE data and observed pKa values of carboxylic acid groups.
Links	PubMed
Keywords	Amino Acid Sequence; Escherichia coli/enzymology; Hydrogen; Hydrogen-Ion Concentration; Macromolecular Substances; Magnetic Resonance Spectroscopy/methods; Molecular Sequence Data; Nitrogen Isotopes; Protein Conformation; Proton-Translocating ATPases/chemistry
edit table

Significance

You can help EcoliWiki by summarizing why this paper is useful

You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.

Add links to pages that link here (e.g. gene, product, method pages)

See Help:References for how to manage references in EcoliWiki.