title: Three-dimensional structure of bradykinin in SDS micelles. Study using nuclear magnetic resonance, distance geometry, and restrained molecular mechanics and dynamics.
abstract: The conformational properties of bradykinin in five molar excess sodium dodecyl sulfate (SDS) micelles have been examined by two-dimensional nuclear magnetic resonance (NMR) techniques at 500 MHz. Detailed structural information for bradykinin in SDS was obtained from quantitative 2-D nuclear Overhauser enhancement (n.O.e.) analyses, distance geometry, and restrained molecular mechanics and dynamics calculations. The conformation of bradykinin in SDS micelles, as determined by these methods, is characterized by a beta-turn-like structure at residues 6-9. A detailed comparison of the structures derived from distance geometry and restrained molecular mechanics and dynamics is also presented.
authors.affiliation: Procter & Gamble Company, Miami Valley Laboratories, Cincinnati, OH.
authors.forename: S C
authors.initials: SC
authors.lastname: Lee
authors.forename: A F
authors.initials: AF
authors.lastname: Russell
authors.forename: W D
authors.initials: WD
authors.lastname: Laidig
mesh_terms: D000595:Amino Acid Sequence; D001920:Bradykinin; D009682:Magnetic Resonance Spectroscopy; D008823:Micelles; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011522:Protons; D012967:Sodium Dodecyl Sulfate; D013816:Thermodynamics
chemical_list: D008823:Micelles; D011522:Protons; D012967:Sodium Dodecyl Sulfate; D001920:Bradykinin