The lubricant of life: A proposal that solvent water promotes extremely fast conformational fluctuations in mobile heteropolypeptide structure
The lubricant of life: A proposal that solvent water promotes extremely fast conformational fluctuations in mobile heteropolypeptide structure
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DOI：
10.1021/bi971323j
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发表时间：
1997-10-28
期刊：
影响因子：
2.9
通讯作者：
Wilson, G
中科院分区：
文献类型：
--
作者：
Barron, LD;Hecht, L;Wilson, G
最近使用拉曼光学活性的新技术进行的观察表明，未折叠蛋白质和熔融球状状态的无序环区域中的单个残基聚集在拉玛钱德朗表面的α-螺旋、β-结构和PPII-螺旋区域中，并且它们在这些区域之间以室温下类似于10（12）s（-1）的速率“闪烁"。有人建议，这些快速运动，发生在相同的皮秒时间尺度上的氢键网络在散装水的重排，促进溶剂水分子通过一个剧目的瞬态水合反转构象。这一建议的蛋白质折叠和功能的一些影响进行了讨论。
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 similar to 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.