Lee S C, Russell A F, Laidig W D
Procter & Gamble Company, Miami Valley Laboratories, Cincinnati, OH.
Int J Pept Protein Res. 1990 May;35(5):367-77.
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.
通过500兆赫的二维核磁共振（NMR）技术，研究了在五摩尔过量十二烷基硫酸钠（SDS）胶束中缓激肽的构象特性。从定量二维核Overhauser增强（n.O.e.）分析、距离几何以及受限分子力学和动力学计算中获得了SDS中缓激肽的详细结构信息。通过这些方法确定的SDS胶束中缓激肽的构象，其特征在于6-9位残基处有一个类似β-转角的结构。还对从距离几何以及受限分子力学和动力学得出的结构进行了详细比较。
