title: Measurement of one-bond 1H-13C, couplings in backbone-labelled proteins.
abstract: NMR dipole-dipole couplings between protein backbone nuclei (1H(alpha), 13C(alpha), 15N, 1H(N), 13C') offer enormous scope for the rapid determination of protein global folds. Here, we show that measurement of one-bond splittings in the protein backbone is facilitated by use of protein that is selectively isotopically enriched only in the backbone atoms. In particular, 1H(alpha)-13C(alpha) couplings can be measured simply and with high sensitivity by use of conventional heteronuclear single quantum correlation (HSQC) techniques.
authors.affiliation: School of Biochemistry and Molecular Biology, University of Leeds, UK.
authors.forename: A W
authors.initials: AW
authors.lastname: Giesen
authors.forename: L C
authors.initials: LC
authors.lastname: Bae
authors.forename: C L
authors.initials: CL
authors.lastname: Barrett
authors.forename: J A
authors.initials: JA
authors.lastname: Chyba
authors.forename: M M
authors.initials: MM
authors.lastname: Chaykovsky
authors.forename: M C
authors.initials: MC
authors.lastname: Cheng
authors.forename: J H
authors.initials: JH
authors.lastname: Murray
authors.forename: E J
authors.initials: EJ
authors.lastname: Oliver
authors.forename: S M
authors.initials: SM
authors.lastname: Sullivan
authors.forename: J M
authors.initials: JM
authors.lastname: Brown
authors.forename: F W
authors.initials: FW
authors.lastname: Dahlquist
authors.forename: S W
authors.initials: SW
authors.lastname: Homans
mesh_terms: D000596:Amino Acids / Q000737:chemistry; D002247:Carbon Isotopes; D006859:Hydrogen; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D014452:Ubiquitins / Q000737:chemistry*
chemical_list: D000596:Amino Acids; D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D014452:Ubiquitins; D006859:Hydrogen