通过氘双量子滤波 NMR 研究弹性蛋白中水的动力学特性。
Investigation of the dynamical properties of water in elastin by deuterium Double Quantum Filtered NMR.
机构信息
Brooklyn College, Department of Physics, 2900 Bedford Avenue Brooklyn, NY 11210, United States.
出版信息
J Magn Reson. 2010 Jul;205(1):86-92. doi: 10.1016/j.jmr.2010.04.007. Epub 2010 Apr 18.
Abstract
The anisotropic motion of tightly bound waters of hydration in bovine nuchal ligament elastin has been studied by deuterium Double Quantum Filtered (DQF) NMR. The experiments have allowed for a direct measurement of the degree of anisotropy within pores of elastin over a time scale ranging from 100 micros to 30 ms, corresponding to a tortuous spatial displacement ranging from 0.2 to 7 microm. We studied the anisotropic motion of deuterium nuclei in D2O hydrated elastin over a temperature of -15 degrees C to 37 degrees C and in solvents with varying dielectric constants. Our experimental measurements of the residual quadrupolar interaction as a function of temperature are correlated to the existing notion of hydrophobic collapse near 20 degrees C.
摘要
牛颈韧带弹性蛋白中紧密结合的水合作用的各向异性运动已通过氘双量子过滤（DQF）NMR 进行了研究。该实验允许在从 100 微秒到 30 毫秒的时间范围内直接测量弹性蛋白孔内各向异性的程度，对应于从 0.2 到 7 微米的曲折空间位移。我们研究了在-15°C 至 37°C 的温度下以及在具有不同介电常数的溶剂中，D2O 水合弹性蛋白中氘核的各向异性运动。我们对残余四极相互作用随温度的变化的实验测量与现有关于在 20°C 附近的疏水性塌陷的概念相关联。
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