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Low-Frequency Protein Motions Coupled to Catalytic Sites.
Annual Review of Physical Chemistry ( IF 11.7 ) Pub Date : 2020-04-20 , DOI: 10.1146/annurev-physchem-050317-014308
Christopher M Cheatum 1
Affiliation  

This review examines low-frequency vibrational modes of proteins and their coupling to enzyme catalytic sites. That protein motions are critical to enzyme function is clear, but the kinds of motions present in proteins and how they are involved in function remain unclear. Several models of enzyme-catalyzed reaction suggest that protein dynamics may be involved in the chemical step of the catalyzed reaction, but the evidence in support of such models is indirect. Spectroscopic studies of low-frequency protein vibrations consistently show that there are underdamped modes of the protein with frequencies in the tens of wavenumbers where overdamped behavior would be expected. Recent studies even show that such underdamped vibrations modulate enzyme active sites. These observations suggest that increasingly sophisticated spectroscopic methods will be able to unravel the link between low-frequency protein vibrations and enzyme function.

中文翻译:

低频蛋白质运动耦合到催化位点。

本文综述了蛋白质的低频振动模式及其与酶催化位点的耦合。蛋白质运动对酶的功能至关重要,但目前尚不清楚蛋白质中存在的运动种类以及它们如何参与功能。几种酶催化反应模型表明,蛋白质动力学可能与催化反应的化学步骤有关,但支持这种模型的证据是间接的。低频蛋白质振动的光谱研究一致表明,存在蛋白质的阻尼不足模式,其频率在数十个波数中,有望发生过度阻尼行为。最近的研究甚至表明,这种衰减不足的振动会调节酶的活性位点。
更新日期:2020-04-21
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