title: Determination of local conformational stability in fragment 96-133 of bovine growth hormone by high-resolution H NMR spectroscopy.
abstract: The specific assignment of resonances in the 400-MHz nuclear magnetic resonance (NMR) spectrum of fragment 96-133 (AII) of bovine growth hormone (bSt) is described. Assignments have been made with homonuclear two-dimensional techniques, in particular that of sequential resonance assignment. Complete assignments were possible for the spin systems of 16 residues out of a total of 38 and partial assignments for another 5. Assignment of resonances to either residue type or a class of residue was possible for a number of other spin systems. Analysis of the type of nuclear Overhauser effect (NOE) indicates that segments 96-110 and 130-133 are nonregular stable structures and that the segment 111-127, which putatively spans the alpha-helix, is not sufficiently stable to generate NOEs.
authors.affiliation: Control Division, Upjohn Company, Kalamazoo, Michigan 49001.
authors.forename: P R
authors.initials: PR
authors.lastname: Gooley
authors.forename: S M
authors.initials: SM
authors.lastname: Plaisted
authors.forename: D N
authors.initials: DN
authors.lastname: Brems
authors.forename: N E
authors.initials: NE
authors.lastname: MacKenzie
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D004355:Drug Stability; D013006:Growth Hormone; D006859:Hydrogen; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D010446:Peptide Fragments; D011487:Protein Conformation; D014357:Trypsin
chemical_list: D010446:Peptide Fragments; C055398:somatotropin fragment 96-133; D006859:Hydrogen; D013006:Growth Hormone; D014357:Trypsin