直接测量机械应变弹性蛋白中蛋白质骨架和近端水合水的相关动力学
Direct measurement of the correlated dynamics of the protein-backbone and proximal waters of hydration in mechanically strained elastin
摘要：
我们报告的相关时间的蛋白质骨架碳和近端水的机械应变弹性蛋白的核磁共振方法的直接测量。实验数据表明，随着生物聚合物上的应变的增加，羰基碳的相关时间减少。这些观察结果与弹性蛋白模拟肽（VPGVG）3的短4ns分子动力学模拟吻合得很好。实验结果还表明，减少近端水化的相关时间，增加应变施加到弹性体。一个简单的模型，建议相关的增加近端水的水化的蛋白质骨架的振动频率的增加，随着应变的增加而发展的运动。总之，蛋白质熵的减少伴随着随着应变的增加而增加的近端水化的熵，支持这样的概念，即弹性的来源是由蛋白质骨架的熵变化引起的熵机制驱动的。
英文摘要：
We report on the direct measurement of the correlation times of the protein backbone carbons and proximal waters of hydration in mechanically strained elastin by nuclear magnetic resonance methods. The experimental data indicate a decrease in the correlation times of the carbonyl carbons as the strain on the biopolymer is increased. These observations are in good agreement with short 4ns molecular dynamics simulations of (VPGVG)3, a well studied mimetic peptide of elastin. The experimental results also indicate a reduction in the correlation time of proximal waters of hydration with increasing strain applied to the elastomer. A simple model is suggested that correlates the increase in the motion of proximal waters of hydration to the increase in frequency of libration of the protein backbone that develops with increasing strain. Together, the reduction in the protein entropy accompanied with the increase in entropy of the proximal waters of hydration with increasing strain, support the notion that the source of elasticity is driven by an entropic mechanism arising from the change in entropy of the protein backbone.
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