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连接蛋白丝的弹性特性和β-折叠结构。

Elastic properties and beta-sheet structure of connectin threads.

作者信息

Mitsui Y, Higuchi H, Terashima S, Takahashi S, Hu D H, Maruyama K, Noda H

机构信息

Faculty of Pharmaceutical Science, University of Tokyo.

出版信息

J Biochem. 1987 Dec;102(6):1483-7. doi: 10.1093/oxfordjournals.jbchem.a122195.

Abstract

Connectin is a very long and flexible protein of striated muscle, linking myosin filaments to z discs in a sarcomere. Isolated native connectin in solution frequently forms elastic threads upon concentration of the solution, by side-by-side association of molecules. An X-ray diffraction study was performed to examine the presence of beta-sheet structure in artificially prepared threads. The elastic properties of such threads were measured at various temperatures. Negative temperature dependence of the elastic coefficient suggests that the elasticity of connectin threads is due to deformation of the three-dimensional structure and not to rubber-like behavior.

摘要

联结蛋白是一种存在于横纹肌中的非常长且具有柔韧性的蛋白质,它在肌节中将肌球蛋白丝与Z盘连接起来。溶液中的天然分离联结蛋白在溶液浓缩时经常会通过分子间并排缔合形成弹性丝。进行了一项X射线衍射研究,以检测人工制备的丝中β-折叠结构的存在。在不同温度下测量了这些丝的弹性特性。弹性系数的负温度依赖性表明,联结蛋白丝的弹性是由于三维结构的变形,而不是类橡胶行为。

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