Rigidity, secondary structure, and the universality of the boson peak in proteins.
Rigidity, secondary structure, and the universality of the boson peak in proteins.
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DOI：
10.1016/j.bpj.2014.05.009
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发表时间：
2014-06
影响因子：
3.4
通讯作者：
S. Perticaroli;J. Nickels;G. Ehlers;A. Sokolov
中科院分区：
文献类型：
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作者：
S. Perticaroli;J. Nickels;G. Ehlers;A. Sokolov
九种蛋白质和氨基酸的互补中子和光散射结果揭示了刚性和二级结构在确定蛋白质低频集体振动动力学的时间和长度尺度中的作用。这些动力学表现为光谱特征，称为玻色子峰（BP），这是所有无序材料所共有的。我们证明 BP 位置随结构基序系统地缩放，反映了局部刚性：无序蛋白质看起来比 α-螺旋蛋白质更软；比β-折叠蛋白更柔软。我们的分析还揭示了蛋白质和氨基酸混合物中 BP 的通用光谱形状；可叠加在典型玻璃中观察到的形状上。基本物理机制的一致性，与特定的化学成分无关，将BP振动与纳米级异质性联系起来，为粗粒度模拟、结构/刚性关系和新颖应用的蛋白质工程提供了实验基准。
Complementary neutron- and light-scattering results on nine proteins and amino acids reveal the role of rigidity and secondary structure in determining the time- and lengthscales of low-frequency collective vibrational dynamics in proteins. These dynamics manifest in a spectral feature, known as the boson peak (BP), which is common to all disordered materials. We demonstrate that BP position scales systematically with structural motifs, reflecting local rigidity: disordered proteins appear softer thanα-helical proteins; which are softer thanβ-sheet proteins. Our analysis also reveals a universal spectral shape of the BP in proteins and amino acid mixtures; superimposable on the shape observed in typical glasses. Uniformity in the underlying physical mechanism, independent of the specific chemical composition, connects the BP vibrations to nanometer-scale heterogeneities, providing an experimental benchmark for coarse-grained simulations, structure/rigidity relationships, and engineering of proteins for novel applications.