title: Improved resolution in three-dimensional constant-time triple resonance NMR spectroscopy of proteins.
abstract: Two new protocols for the three-dimensional, triple resonance, constant-time HCA(CO)N NMR experiment are presented that significantly increase the experimental resolution attainable in the C alpha frequency dimension. Experimental verification of the new experiments is provided by spectra of the IIA domain of glucose permease from Bacillus subtilis.
authors.affiliation: Department of Molecular Biology, Scripps Research Institute, La Jolla, CA 92037.
authors.forename: A G
authors.initials: AG
authors.lastname: Palmer
authors.forename: W J
authors.initials: WJ
authors.lastname: Fairbrother
authors.forename: J
authors.initials: J
authors.lastname: Cavanagh
authors.forename: P E
authors.initials: PE
authors.lastname: Wright
authors.forename: M
authors.initials: M
authors.lastname: Rance
mesh_terms: D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000201:enzymology; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008433:Mathematics; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System / Q000737:chemistry*; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D013997:Time Factors
chemical_list: D011506:Proteins; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System; C031629:phosphoenolpyruvate-glucose phosphotransferase