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首页> 外文期刊>Applied Magnetic Resonance >Mobility and structure of human serum albumin powders in water-acetonitrile mixtures by H-1 NMR relaxation and FTIR spectroscopy
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Mobility and structure of human serum albumin powders in water-acetonitrile mixtures by H-1 NMR relaxation and FTIR spectroscopy

机译：H-1 NMR弛豫和FTIR光谱分析人血清白蛋白粉在水-乙腈混合物中的流动性和结构

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摘要

The effect of acetonitrile on protein dynamics was investigated for solid human serum albumin samples at various hydration levels. Temperature dependences of H-1 nonselective nuclear magnetic resonance T-1 and T-2 relaxation times at 27 MHz have been measured and data were interpreted in terms of three kinds of internal motions in the protein. Microdynamic parameters of the motions were obtained within a '' model-free '' approach. It was found that acetonitrile hardly affects the fast motions but noticeably influences the slow motion of side chain groups, shortening the correlation time and increasing the amplitude of the motion. The acetonitrile effect on dynamics is likely based on the appearance of additional free volume as a result of the formation of rigid helical parts in the protein structure. Water, plasticizing the protein structure, promotes the action of organic solvent. A definite part of side chain groups, slowly moving in the same frequency window as the rest of protein side chain groups, performs less constrained '' liquidlike '' motion. The relative population of these highly movable protons is closely correlated with the increment of the helical structure induced by water and acetonitrile.
机译：在各种水合水平下，研究了固体人血清白蛋白样品中乙腈对蛋白质动力学的影响。已经测量了H-1非选择性核磁共振T-1和T-2在27 MHz时的弛豫时间的温度依赖性，并根据蛋白质中的三种内部运动解释了数据。运动的微动力参数是通过“无模型”方法获得的。发现乙腈几乎不影响快速运动，但是显着影响侧链基团的慢运动，从而缩短了相关时间并增加了运动幅度。乙腈对动力学的影响很可能是由于蛋白质结构中刚性螺旋部分的形成导致出现了额外的自由体积。水可塑化蛋白质结构，促进有机溶剂的作用。一定数量的侧链基团与其余的蛋白质侧链基团在相同的频率窗口中缓慢移动，执行的约束较少，“液状”运动。这些高度可移动的质子的相对数量与水和乙腈引起的螺旋结构的增加密切相关。

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