水合溶菌酶单粒子弛豫的对数衰减
Logarithmic decay in single-particle relaxations of hydrated lysozyme powder
摘要：
采用分子动力学模拟方法，研究了水合溶菌酶蛋白质氨基酸在生理温度附近的自动力学行为。氨基酸残基质心和蛋白质氢原子的自中间散射函数（SISF）在30年的时间内显示从2皮秒到2纳秒的对数衰减，随后是指数α弛豫。这种缓慢的动力学类似的β-弛豫时间范围内的模式耦合理论（MCT）预测的高阶奇点附近的弛豫方案。这些结果表明，蛋白质的单粒子动力学和胶体，聚合物和分子玻璃形成液体的动力学之间有很强的相似性。
英文摘要：
We present the self-dynamics of protein amino acids of hydrated lysozyme powder around the physiological temperature by means of molecular dynamics (MD) simulations. The self-intermediate scattering functions (SISF) of the amino acid residue center-of-mass and of the protein hydrogen atoms display a logarithmic decay over 3 decades of time, from 2 picoseconds to 2 nanoseconds, followed by an exponential alpha-relaxation. This kind of slow dynamics resembles the relaxation scenario within the beta-relaxation time range predicted by the mode coupling theory (MCT) in the vicinity of higher-order singularities. These results suggest a strong analogy between the single-particle dynamics of the protein and the dynamics of colloidal, polymeric and molecular glass-forming liquids.
机构、总结、中文摘要均由AI分析而来，可能存在错误，请以论文正文为准。
