Biochemistry. Enzymes in coherent motion.
Biochemistry. Enzymes in coherent motion.
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生物化学。
DOI：
10.1126/science.1217170
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发表时间：
2012
期刊：
影响因子：
--
通讯作者：
Lu,HPeter
中科院分区：
文献类型：
--
作者：
Lu,HPeter
微妙的构象变化往往在酶的功能中起着至关重要的作用，酶的构象是高度动态的。因此，仅使用平衡状态下的整体平均测量的静态结构表征通常不足以预测动态构象和理解相关的酶功能。单分子方法研究特定生理条件下的单个分子，是表征和分析复杂酶反应动力学和相关构象动力学的有力工具。在这期杂志的第319页，Choiet等人报道了一种探测单分子构象动力学的新方法，该方法揭示了酶的活性位点在酶促反应翻转过程中的构象运动。
Subtle conformational changes often play a crucial role in enzyme functions, and enzyme conformations are highly dynamic. The use of only a static structural characterization from an ensemble-averaged measurement at equilibrium is therefore often inadequate for predicting dynamic conformations and understanding correlated enzyme functions. Single-molecule approaches , which investigate individual molecules under specific physiological conditions, are a powerful tool for characterizing and analyzing complex enzymatic reaction dynamics and correlated conformational dynamics. On page 319 of this issue, Choiet al.report a novel approach to probing single-molecule conformational dynamics that reveals the conformational motions of the enzyme's active site during enzymatic reaction turnovers.