Barron L D, Hecht L, Wilson G
Chemistry Department, University of Glasgow, U.K.
Biochemistry. 1997 Oct 28;36(43):13143-7. doi: 10.1021/bi971323j.
Recent observations using the novel technique of Raman optical activity suggest that individual residues in unfolded proteins and in disordered loop regions of molten globule-like states cluster in the alpha-helix, beta-structure, and PPII-helix regions of the Ramachandran surface and that they "flicker" between these regions at rates approximately 10(12) s-1 at room temperature. It is proposed that these rapid motions, which occur on the same picosecond time scale as rearrangements of the hydrogen bond network in bulk water, are promoted by solvent water molecules via a repertoire of transient hydrated reverse turn conformations. Some implications of this proposal for protein folding and function are discussed.
最近使用拉曼光学活性新技术的观察结果表明，未折叠蛋白质以及类熔球态无序环区域中的单个残基聚集在拉氏构象图的α螺旋、β结构和PPII螺旋区域，并且它们在室温下以大约10¹² s⁻¹的速率在这些区域之间“闪烁”。有人提出，这些快速运动与大量水中氢键网络的重排发生在相同的皮秒时间尺度上，是由溶剂水分子通过一系列瞬态水合反向转角构象促进的。本文讨论了这一观点对蛋白质折叠和功能的一些影响。
