title: Preferred conformational state of the N-terminus section of a bovine growth hormone fragment (residues 96-133) in water is an omega loop.
abstract: The solution structure of a 38-amino-acid-residue, biologically active fragment of bovine growth hormone (bGH96-133) was investigated with a combined nuclear magnetic resonance (NMR) and computer modeling approach. With the distance geometry program DISGEO and distance constraints derived from nuclear Overhauser enhancement (NOE) experiments, it was found that residues Ser-100 to Tyr-110 circumscribe and omega-loop, a recently categorized feature of nonregular secondary protein structure.
authors.affiliation: Department of Pharmaceutical Sciences, University of Arizona, Tucson 85721.
authors.forename: P R
authors.initials: PR
authors.lastname: Gooley
authors.forename: S A
authors.initials: SA
authors.lastname: Carter
authors.forename: P E
authors.initials: PE
authors.lastname: Fagerness
authors.forename: N E
authors.initials: NE
authors.lastname: MacKenzie
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D003198:Computer Simulation; D013006:Growth Hormone; D008969:Molecular Sequence Data; D011487:Protein Conformation; D014867:Water
chemical_list: D014867:Water; D013006:Growth Hormone