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  • Title: Three-dimensional structure of bradykinin in SDS micelles. Study using nuclear magnetic resonance, distance geometry, and restrained molecular mechanics and dynamics.
    Author: Lee SC, Russell AF, Laidig WD.
    Journal: Int J Pept Protein Res; 1990 May; 35(5):367-77. PubMed ID: 2165467.
    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.
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