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钙调蛋白分子动力学对pH值和离子强度的依赖性。

The dependence of the molecular dynamics of calmodulin upon pH and ionic strength.

作者信息

Steiner R F, Lambooy P K, Sternberg H

出版信息

Arch Biochem Biophys. 1983 Apr 1;222(1):158-69. doi: 10.1016/0003-9861(83)90513-1.

Abstract

The mobilities of several fluorescent probes placed at different locations on calmodulin in the absence of Ca2+ have been found to depend upon the charge, ionic strength, and temperature. In general, the time decay of fluorescence anisotropy could be fitted with two rotational correlation times. The shorter of these reflects primarily the motion of the probe itself, while the longer corresponds to the motion of a major portion of the molecule. An increase in ionic strength or a decrease in net charge results in a decrease in the relative amplitude of the shorter correlation time, while an increase in temperature produces an increase in its amplitude. These results are consistent with, and suggest, that an increase in probe mobility accompanies an expansion of the calmodulin molecule under conditions of high electrostatic stress.

摘要

已发现,在无Ca2+的情况下,放置在钙调蛋白不同位置的几种荧光探针的迁移率取决于电荷、离子强度和温度。一般来说,荧光各向异性的时间衰减可以用两个旋转相关时间来拟合。其中较短的时间主要反映探针本身的运动,而较长的时间则对应于分子主要部分的运动。离子强度增加或净电荷减少会导致较短相关时间的相对振幅降低,而温度升高则会使其振幅增加。这些结果与以下观点一致,并表明在高静电应力条件下,随着钙调蛋白分子的扩张,探针迁移率增加。

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