title: Complete 1H and 13C assignment of Lys and Leu sidechains of staphylococcal nuclease using HCCH-COSY and HCCH-TOCSY 3D NMR spectroscopy.
abstract: Complete proton and carbon sidechain assignments are reported for 22 lysine and 11 leucine residues in staphylococcal nuclease, an enzyme with 149 residues. These assignments are readily obtained in a direct manner from the correlations observed in the 3D HCCH-COSY and HCCH-TOCSY spectra and the known protein backbone assignments. These assignments open the way to detailed studies of the sidechain structure and dynamics at the active site, in the hydrophobic core and on the surface of the protein.
authors.affiliation: Bone Research Branch, National Institute of Dental Research, National Institutes of Health, Bethesda, MD 20892.
authors.forename: D M
authors.initials: DM
authors.lastname: Baldisseri
authors.forename: J G
authors.initials: JG
authors.lastname: Pelton
authors.forename: S W
authors.initials: SW
authors.lastname: Sparks
authors.forename: D A
authors.initials: DA
authors.lastname: Torchia
mesh_terms: D002247:Carbon Isotopes; D006859:Hydrogen; D007930:Leucine; D008239:Lysine; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008836:Micrococcal Nuclease / Q000737:chemistry*; D011487:Protein Conformation
chemical_list: D002247:Carbon Isotopes; D006859:Hydrogen; D008836:Micrococcal Nuclease; D007930:Leucine; D008239:Lysine