Translational and rotational diffusion of a small globular protein under crowded conditions.

Translational and rotational diffusion of a small globular protein under crowded conditions.
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DOI:
10.1021/jp907744m
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发表时间:
2009-10-08
期刊:
The journal of physical chemistry. B
影响因子:
--
通讯作者:
Pielak GJ
Pielak GJ
中科院分区:
其他
文献类型:
--
作者:
Li C;Wang Y;Pielak GJ

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蛋白质相互作用是生物信号转导的基本步骤。相互作用的蛋白质通过扩散找到彼此。为了深入了解扩散拥挤的条件下发现在细胞中,我们使用核磁共振光谱(NMR)来测量的7.4 kDa的球状蛋白质,胰凝乳蛋白酶抑制剂2的平移和旋转扩散的溶剂添加剂的影响。添加剂为甘油和大分子拥挤剂聚乙烯吡咯烷酮(PVP)。随着溶液粘度的增加,平移扩散和旋转扩散均减小。对于甘油,减少遵守斯托克斯爱因斯坦和斯托克斯爱因斯坦德拜定律。PVP观察到三种类型的偏差:随着粘度的增加,扩散的减少小于预测,这种负偏差更大的旋转扩散,和负偏差随着PVP分子量的增加而增加。我们讨论了我们的结果在其他研究的大分子对球状蛋白质扩散的影响。
Protein protein interaction is the fundamental step of biological signal transduction. Interacting proteins find each other by diffusion. To gain insight into diffusion under the crowded conditions found in cells, we used nuclear magnetic resonance spectroscopy (NMR) to measure the effects of solvent additives on the translational and rotational diffusion of the 7.4 kDa globular protein, chymotrypsin inhibitor 2. The additives were glycerol and the macromolecular crowding agent, polyvinylpyrrolidone (PVP). Both translational diffusion and rotational diffusion decrease with increasing solution viscosity. For glycerol, the decrease obeys the Stokes Einstein and Stokes Einstein Debye laws. Three types of deviation are observed for PVP: the decrease in diffusion with increased viscosity is less than predicted, this negative deviation is greater for rotational diffusion, and the negative deviation increases with increasing PVP molecular weight. We discuss our results in terms of other studies on the effects of macromolecules on globular protein diffusion.
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