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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >The unusually stable coiled-coil domain of COMP exhibits cold and heat denaturation in 4-6 M guanidinium chloride
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The unusually stable coiled-coil domain of COMP exhibits cold and heat denaturation in 4-6 M guanidinium chloride

机译：COMP的异常稳定的盘绕域在4-6 M氯化胍中表现出冷和热变性

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摘要

A high thermal stability is observed for the five-stranded alpha-helical coiled-coil domain of cartilage oligomeric matrix protein COMP. It does not unfold in non-denaturing buffer between 0 and 100 degrees C and thermal denaturation is only achieved at high concentrations of guanidinium chloride (4-6 M). In these solutions the protein structure is lost at decreasing (cold denaturation) and increasing temperatures (heat denaturation). In the cold denaturation region, the melting pro file showed deviations from the theory of Privalov et al. [P.L. Privalov, V. Griko Yu, S. Venyaminov, V.P. Kutyshenko, Cold denaturation of myoglobin, J. Mol. Biol. 190 (1986) 487-498] probably due to deviations from a two-state mechanism. High thermal stability as well as cold and heat denaturation was also observed for a mutant of the coiled-coil domain of COMP in which glutamine 54 was replaced by isoleucine but it still forms pentamer. The melting temperatures in plain buffer for the heat denaturation of COMP coiled-coil domain and its mutant obtained by extrapolation to zero molar guanidinium chloride concentration are approximately 160 and 220 degrees C, respectively which groups them among the most stable proteins. (C) 2000 Elsevier Science B.V. All rights reserved. [References: 32]
机译：对于软骨寡聚基质蛋白COMP的五链α-螺旋卷曲螺旋结构域观察到高的热稳定性。它不会在0至100摄氏度之间的非变性缓冲液中展开，并且仅在高浓度的氯化胍（4-6 M）时才能实现热变性。在这些溶液中，蛋白质结构在降低（冷变性）和升高温度（热变性）时丧失。在冷变性区，熔化曲线表明与Privalov等人的理论存在偏差。 [P.L. Privalov，V.Griko Yu，S.Venaminov，V.P. Kutyshenko，肌红蛋白的冷变性，J。Mol。生物学190（1986）487-498]可能是由于偏离了两种状态机制。还观察到COMP的卷曲螺旋结构域的突变体的高热稳定性以及冷和热变性，其中谷氨酰胺54被异亮氨酸代替，但是它仍然形成五聚体。用于COMP卷曲螺旋结构域热变性的普通缓冲液及其突变体的外推温度约为160℃和220℃，这是通过外推至零摩尔氯化胍浓度获得的，这将它们归类为最稳定的蛋白质。 （C）2000 Elsevier Science B.V.保留所有权利。 [参考：32]

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