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首页> 外文期刊>International Journal of Biological Macromolecules: Structure, Function and Interactions >Guanidine-induced unfolding of the Sso7d protein from the hyperthermophilic archaeon Sulfolobus solfataricus
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Guanidine-induced unfolding of the Sso7d protein from the hyperthermophilic archaeon Sulfolobus solfataricus

机译：胍诱导的超嗜热古细菌Sulfolobus solfataricus的Sso7d蛋白解折叠。

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摘要

The unfolding induced by guanidine hydrochloride of the small protein Sso7d from the hyperthermophilic archaeon Sulfolobus solfataricus has been investigated by means of circular dichroism and fluorescence measurements. At neutral pH and room temperature the midpoint of the transition occurred at 4M guanidine hydrochloride. Thermodynamic information was obtained by means of both the linear extrapolation model and the denaturant binding model, in the assumption of a two-state N double left right arrow D transition. A comparison with thermodynamic data determined from the thermal unfolding of Sso7d indicated that the denaturant binding model has to be preferred. Finally, it is shown that Sso7d is the most stable against both temperature and guanidine hydrochloride among a set of globular proteins possessing a very similar 3D structure. (C) 2004 Elsevier B.V. All rights reserved.
机译：通过圆二色性和荧光测量研究了盐酸胍诱导的超嗜热古细菌Sulfolobus solfataricus的小蛋白Sso7d的解折叠。在中性pH和室温下，转变的中点发生在4M盐酸胍中。在两态N双向左向右向右D过渡的假设下，通过线性外推模型和变性剂结合模型获得热力学信息。与根据Sso7d的热展开确定的热力学数据的比较表明，变性剂结合模型必须是首选的。最后，表明在一组具有非常相似的3D结构的球形蛋白质中，Sso7d对温度和盐酸胍最稳定。 （C）2004 Elsevier B.V.保留所有权利。

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