蛋白质能量景观粗糙度的直接测量。
Direct measurement of protein energy landscape roughness.
作者信息
Nevo Reinat, Brumfeld Vlad, Kapon Ruti, Hinterdorfer Peter, Reich Ziv
机构信息
Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel.
出版信息
EMBO Rep. 2005 May;6(5):482-6. doi: 10.1038/sj.embor.7400403.
Abstract
The energy landscape of proteins is thought to have an intricate, corrugated structure. Such roughness should have important consequences on the folding and binding kinetics of proteins, as well as on their equilibrium fluctuations. So far, no direct measurement of protein energy landscape roughness has been made. Here, we combined a recent theory with single-molecule dynamic force spectroscopy experiments to extract the overall energy scale of roughness epsilon for a complex consisting of the small GTPase Ran and the nuclear transport receptor importin-beta. The results gave epsilon > 5k(B)T, indicating a bumpy energy surface, which is consistent with the ability of importin-beta to accommodate multiple conformations and to interact with different, structurally distinct ligands.
摘要
蛋白质的能量景观被认为具有复杂的、起伏不平的结构。这种粗糙度应该会对蛋白质的折叠和结合动力学以及它们的平衡涨落产生重要影响。到目前为止，尚未对蛋白质能量景观的粗糙度进行直接测量。在这里，我们将最近的理论与单分子动态力谱实验相结合，以提取由小GTP酶Ran和核转运受体输入蛋白β组成的复合物的整体粗糙度能量尺度ε。结果给出ε>5k(B)T，表明能量表面崎岖不平，这与输入蛋白β容纳多种构象并与不同的、结构不同的配体相互作用的能力一致。
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本文引用的文献
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