Microwave based reversible unfolding and refolding of alcohol oxidase protein probed by fluorescence and circular dichroism spectroscopy

Somasekhar R. Chinnadayyala, M. Santhosh, P. Goswami
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引用次数: 4

Abstract

The reversible effect of microwave mediated denaturation of protein at low exposure time of 10 s has been demonstrated for the first time. The effect of microwave (2.45 GHz and 900 W) was confirmed in a homo-octameric alcohol oxidase in aqueous solution of pH 7.5. The unfolding events did not transverse through any intermediate states and no subunits of the protein were detached during the process. The refolding of the protein achieved at 4℃ for 24 h had regenerated the native enzyme. This reversible refolding approach excludes any chemical reagent and therefore established as simple technique for protein unfolding-folding studies.
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用荧光和圆二色光谱研究微波基酒精氧化酶蛋白的可逆展开和再折叠
本文首次证实了微波介导蛋白质在低暴露时间10s下变性的可逆效应。在pH为7.5的水溶液中,证实了微波(2.45 GHz, 900 W)对同型八聚醇氧化酶的影响。在此过程中,展开事件没有横向通过任何中间状态,也没有蛋白质的亚基分离。在4℃、24 h条件下对蛋白质进行再折叠,使原酶再生。这种可逆的再折叠方法排除了任何化学试剂,因此被确立为蛋白质展开折叠研究的简单技术。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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