THE ENERGY LANDSCAPES AND MOTIONS OF PROTEINS
THE ENERGY LANDSCAPES AND MOTIONS OF PROTEINS
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DOI：
10.1126/science.1749933
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发表时间：
1991-12-13
期刊：
影响因子：
56.9
通讯作者：
WOLYNES, PG
中科院分区：
文献类型：
--
作者：
FRAUENFELDER, H;SLIGAR, SG;WOLYNES, PG
最近的实验，理论上的进步，以及与其他复杂系统（如玻璃和自旋玻璃）的类比，使人们对蛋白质动力学有了深入的了解。理解的基础是观察到能量景观是复杂的：蛋白质可以采取大量的近等能构象（构象亚态）。从构象亚态和它们之间的运动的研究中出现的概念，允许一个简单的反应，如一氧化碳的小配体结合肌红蛋白的定量讨论。
Recent experiments, advances in theory, and analogies to other complex systems such as glasses and spin glasses yield insight into protein dynamics. The basis of the understanding is the observation that the energy landscape is complex: Proteins can assume a large number of nearly isoenergetic conformations (conformational substates). The concepts that emerge from studies of the conformational substates and the motions between them permit a quantitative discussion of one simple reaction, the binding of small ligands such as carbon monoxide to myoglobin.