Three-dimensional structure of bradykinin in SDS micelles. Study using nuclear magnetic resonance, distance geometry, and restrained molecular mechanics and dynamics.
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.
Lee
S C
SC
Procter & Gamble Company, Miami Valley Laboratories, Cincinnati, OH.
Russell
A F
AF
Laidig
W D
WD
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
D008823:Micelles; D011522:Protons; D012967:Sodium Dodecyl Sulfate; D001920:Bradykinin