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首页> 外文期刊>Journal of Molecular Biology >INTRINSIC STABILITY OF INDIVIDUAL ALPHA HELICES MODULATES STRUCTURE AND STABILITY OF THE APOMYOGLOBIN MOLTEN GLOBULE FORM
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INTRINSIC STABILITY OF INDIVIDUAL ALPHA HELICES MODULATES STRUCTURE AND STABILITY OF THE APOMYOGLOBIN MOLTEN GLOBULE FORM

机译：单个α子的内在稳定性调节了淀粉球蛋白融合球形式的结构和稳定性

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摘要

During acid-induced unfolding of apomyoglobin, a partly folded form is observed at pH values of around four. In this form, the A, G and H helices are folded, while the rest of the molecule, including the B helix, demonstrates Little structure. The partly folded form has been described as a molten globule form. To determine the factors that govern the structure and stability of this form, we introduced two helix-stabilizing mutations into the B helix, and tested their effect on the structure and stability of both the native form and the molten globule form. We show that the two Gly --> Ala replacements in the B helix produce altered fluorescence and CD properties of the partly folded intermediate, a result which implies that the B helix has become part of the structured region of the molten globule form. The helix content of a model peptide containing the sequence of the B helix is increased by the G --> A replacements, as is the helix content of the molten globule intermediate, whereas the stability and the helix content of the native protein are not altered. The observed increase in helicity is larger in the folding intermediate than in the model peptide, suggesting that nonspecific interactions, such as the hydrophobic interactions exhibited by the entire polypeptide chain, amplify the effect of intrinsic helix stability The overall results suggest that the intrinsic stability of each individual helix is a factor in deciding whether or not that helix becomes part of the structured molten globule. (C) 1995 Academic Press Limited [References: 40]
机译：在酸诱导的肌红蛋白解折叠过程中，在约4的pH值下观察到部分折叠的形式。以这种形式，A，G和H螺旋被折叠，而分子的其余部分（包括B螺旋）表现出Little结构。已将部分折叠的形式描述为熔融小球形式。为了确定控制这种形式的结构和稳定性的因素，我们在B螺旋中引入了两个螺旋稳定突变，并测试了它们对天然形式和熔融小球形式的结构和稳定性的影响。我们显示B螺旋中的两个Gly-> Ala置换产生部分折叠的中间体的荧光和CD性质发生改变，结果表明B螺旋已成为熔融小球形式的结构化区域的一部分。包含B螺旋序列的模型肽的螺旋含量通过G-> A替换而增加，熔融小球中间体的螺旋含量也是如此，而天然蛋白的稳定性和螺旋含量没有改变。在折叠中间体中观察到的螺旋度增加比在模型肽中大，这表明非特异性相互作用（例如整个多肽链表现出的疏水相互作用）放大了固有螺旋稳定性的影响。总体结果表明，螺旋的固有稳定性每个单独的螺旋都是决定该螺旋是否成为结构化熔融小球的一部分的因素。 （C）1995 Academic Press Limited [参考：40]

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