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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Analysis of hydrophobic and charged patches and influence of medium- and long-range interactions in molecular chaperones.
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Analysis of hydrophobic and charged patches and influence of medium- and long-range interactions in molecular chaperones.

机译:分析疏水和带电斑块以及分子伴侣中的中长期相互作用的影响。

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摘要

The amino acid composition of the aromatic residues Phe, Tyr and Trp are much less significant in chaperones and the residues Cys, Glu, His, Met and Pro vary significantly in chaperones compared to normal globular proteins. In the present work, we have analysed the hydrophobic and charged patches in molecular chaperones which provide more insight for a better understanding of chaperone folding. Also, we have investigated the role of medium- and long-range contacts in chaperones and the preference of amino acid residues influenced by these interactions. Furthermore, the role of hydrophobic and helix-forming residues and disulfide bonding in these interactions have been discussed.
机译:与伴侣球蛋白相比,伴侣蛋白中芳香族残基Phe,Tyr和Trp的氨基酸组成不那么重要,而伴侣蛋白中的Cys,Glu,His,Met和Pro残基则有很大差异。在目前的工作中,我们已经分析了分子伴侣中的疏水和带电补丁,为更好地了解伴侣折叠提供了更多的见识。此外,我们研究了分子伴侣中和远程接触的作用以及受这些相互作用影响的氨基酸残基的偏好。此外,已经讨论了疏水和螺旋形成残基以及二硫键在这些相互作用中的作用。

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