Unraveling multistate unfolding of rabbit muscle creatine kinase

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology Pub Date : 2002-04-01 DOI:10.1016/S0167-4838(02)00212-1

Irina M Kuznetsova , Olga V Stepanenko, Konstantin K Turoverov , Li Zhu , Jun-Mei Zhou , Anthony L Fink , Vladimir N Uversky

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引用次数: 87

Abstract

GdmCl-induced unfolding of rabbit muscle creatine kinase, CK, has been studied by a variety of physico-chemical methods including near and far UV CD, SEC, intrinsic fluorescence (intensity, anisotropy and lifetime) as well as intensity and lifetime of bound ANS fluorescence. The formation of several stable unfolding intermediates, some of which were not observed previously, has been established. This was further confirmed by representation of fluorescence data in terms of ‘phase diagram’, i.e. I_λ1 versus I_λ2 dependence, where I_λ1 and I_λ2 are fluorescence intensity values measured on wavelengths λ₁ and λ₂ under the different experimental conditions for a protein undergoing structural transformations. The unfolding behavior of CK was shown to be strongly affected by association of partially folded intermediates. A model of CK unfolding, which takes into account both structural perturbations and association of partially folded intermediates has been elaborated.

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揭示兔肌肌酸激酶的多态展开

采用多种物理化学方法，包括近、远紫外CD、SEC、本征荧光(强度、各向异性和寿命)以及结合ANS荧光的强度和寿命，研究了gdml诱导兔肌酸激酶(CK)的展开。已经确定了几种稳定的展开中间体的形成，其中一些是以前没有观察到的。荧光数据的“相图”表示进一步证实了这一点，即Iλ1与Iλ2依赖关系，其中Iλ1和Iλ2是在不同实验条件下对波长λ1和λ2进行结构转化的蛋白质测量的荧光强度值。CK的展开行为受到部分折叠中间体缔合的强烈影响。提出了一种考虑结构扰动和部分折叠中间体关联的CK展开模型。

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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Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology

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