Universality and Structural Implications of the Boson Peak in Proteins
Universality and Structural Implications of the Boson Peak in Proteins
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DOI：
10.1016/j.bpj.2019.06.007
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发表时间：
2019-07-23
影响因子：
3.4
通讯作者：
Kataoka, Mikio
中科院分区：
文献类型：
--
作者：
Nakagawa, Hiroshi;Joti, Yasumasa;Kataoka, Mikio
蛋白质的柔软性和刚性反映在结构动力学上，而结构动力学又受到环境的影响。蛋白质的特征低频振动谱（称为玻色子峰）是蛋白质在低温或脱水条件下结构刚性的指标。在本文中，通过使用非弹性中子散射和分子动力学模拟来评估水合、温度和压力对球状蛋白的玻色子峰和体积特性的影响。水合、加压和冷却将玻色子峰位置移至更高能量并降低峰强度并减少蛋白质和空腔体积。我们发现了蛋白质中玻色子峰和空腔体积之间的相关性。腔体体积的减小意味着刚性的增加，这就是玻色子峰移的根源。玻色子峰是蛋白质的普遍性质，通过相关性合理化。
The softness and rigidity of proteins are reflected in the structural dynamics, which are in turn affected by the environment. The characteristic low-frequency vibrational spectrum of a protein, known as boson peak, is an indication of the structural rigidity of the protein at a cryogenic temperature or dehydrated conditions. In this article, the effect of hydration, temperature, and pressure on the boson peak and volumetric properties of a globular protein are evaluated by using inelastic neutron scattering and molecular dynamics simulation. Hydration, pressurization, and cooling shift the boson peak position to higher energy and depress the peak intensity and decreases the protein and cavity volumes. We found the correlation between the boson peak and cavity volume in a protein. A decrease of cavity volume means the increase of rigidity, which is the origin of the boson peak shift. Boson peak is the universal property of a protein, which is rationalized by the correlation.