Kline A D, Braun W, Wüthrich K
J Mol Biol. 1986 May 20;189(2):377-82. doi: 10.1016/0022-2836(86)90519-x.
This is a preliminary report on the determination of the solution conformation of the alpha-amylase inhibitor Tendamistat by nuclear magnetic resonance and distance geometry calculations. A characterization is given of the complete polypeptide backbone fold and the side-chains of the presumed active site in this protein. These results are based on complete sequence-specific resonance assignments, a list of 401 distance constraints from nuclear Overhauser effects, 168 distance constraints from hydrogen bonds and disulphide bridges, and 50 torsion angle constraints from measurements of spin-spin coupling constants.
这是一篇关于通过核磁共振和距离几何计算确定α-淀粉酶抑制剂 Tendamistat 溶液构象的初步报告。文中给出了该蛋白质完整多肽主链折叠以及假定活性位点侧链的特征描述。这些结果基于完整的序列特异性共振归属、401 个来自核 Overhauser 效应的距离约束列表、168 个来自氢键和二硫键桥的距离约束以及 50 个来自自旋-自旋耦合常数测量的扭转角约束。
