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[胶原蛋白分子螺旋部分中热稳定结构域的存在]

[The presence of a thermally stable domain in the spiral part of a collagen molecule].

作者信息

Burdzhanadze T V, Lomaia M A, Bezhitadze M O

出版信息

Biofizika. 1989 May-Jun;34(3):377-83.

PMID:2765568
Abstract

It is shown that in 0,5 M NaCl 8 M CH3COOH heat absorption and the second structure alteration in a heated solution proceed between two stages following one another, and besides, salts not only decrease the macromolecule denaturation temperature in total, but produce different destabilization effect on different regions. The presence of the thermostable domain in the macromolecule helical part permits investigation of the folding mechanism of the triple collagen helix under partial denaturation. The localization and biological role of the stable domain in the triple helix formation are suggested.

摘要

结果表明,在0.5M NaCl、8M CH3COOH溶液中,热吸收和加热溶液中的二级结构变化在相继的两个阶段之间进行,此外,盐不仅总体上降低了大分子变性温度,而且对不同区域产生不同的去稳定作用。大分子螺旋部分中热稳定结构域的存在使得能够研究部分变性条件下三股胶原螺旋的折叠机制。文中还提出了稳定结构域在三股螺旋形成中的定位及其生物学作用。

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