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[α-原肌球蛋白及其片段的热变性]

[Heat denaturation of alpha-tropomyosin and its fragments].

作者信息

Potekhin S A, Privalov P L

出版信息

Biofizika. 1978 Mar-Apr;23(2):219-23.

PMID:647030
Abstract

The reasons for three heterogeneity of tropomyosin melting curves are considered. It is shown that this phenomenon is due to the molecular heterogeneity of the preparation. Different states of the SH-groups as well as the different stability of molecule regions. The melting curves of alpha-tropomyosin and two of its fragments are obtained. The thermodynamic parameters stabilizing their helical structure are determined. The existence of a thermodynamical transition at 31 degrees C is shown for alpha-tropomyosin leading to the loss of the ability of the molecule to form supra-molecular structures.

摘要

考虑了原肌球蛋白解链曲线三种异质性的原因。结果表明,这种现象是由于制剂的分子异质性所致。SH基团的不同状态以及分子区域的不同稳定性。获得了α-原肌球蛋白及其两个片段的解链曲线。确定了稳定其螺旋结构的热力学参数。结果表明,α-原肌球蛋白在31℃存在热力学转变,导致分子形成超分子结构的能力丧失。

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