Kudryashov Dmitri S, Reisler Emil
Department of Chemistry and Biochemistry, the Ohio State University, Columbus, OH 43210.
Biopolymers. 2013 Apr;99(4):245-56. doi: 10.1002/bip.22155.
This minireview is dedicated to the memory of Henryk Eisenberg and honors his major contributions to many areas of biophysics and to the analysis of macromolecular states and interactions in particular. This work reviews the ATP and ADP states of a ubiquitous protein, actins, and considers the present evidence for and against unique, nucleotide-dependent conformations of this protein. The effects of ATP and ADP on specific structural elements of actins, its loops and clefts, as revealed by mutational, crosslinking, spectroscopic, and EPR methods are discussed. It is concluded that the existing evidence points to dynamic equilibria of these structural elements among various conformational states in both ATP- and ADP-actins, with the nucleotides impacting the equilibria distributions.
这篇短文是为纪念亨利克·艾森伯格而作，以表彰他在生物物理学诸多领域，尤其是大分子状态及相互作用分析方面的重大贡献。本文回顾了一种普遍存在的蛋白质——肌动蛋白的ATP和ADP状态，并考量了目前支持和反对该蛋白存在独特的、依赖核苷酸构象的证据。文中讨论了通过突变、交联、光谱学和电子顺磁共振方法所揭示的ATP和ADP对肌动蛋白特定结构元件（其环和裂隙）的影响。得出的结论是，现有证据表明，在ATP - 肌动蛋白和ADP - 肌动蛋白中，这些结构元件在各种构象状态之间存在动态平衡，核苷酸会影响平衡分布。
