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首页> 外文期刊>Biochemistry >A Native Disulfide Stabilizes Non-Native Helical Structures in Partially Folded States of Equine β-Lactoglobulin
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A Native Disulfide Stabilizes Non-Native Helical Structures in Partially Folded States of Equine β-Lactoglobulin

机译：天然二硫化物稳定在β-乳蛋白的部分折叠状态下的非天然螺旋结构

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摘要

Equine β-lactoglobulin (ELG) assumes non-native helices during refolding and in partially folded states. Previously, circular dichroism (CD) combined with site-directed mutagenesis identified helical regions in the acid- and cold-denatured states of ELG. It is also known that a fragment of ELG, CHIBL (residues 88-142), has a structure similar to that of the colddenatured state. For the study reported herein, the structure of a shorter fragment, CHIBLΔF (residues 97-142), was investigated by CD and nuclear magnetic resonance spectroscopy. The secondary chemical shifts clearly showed that non-native α-helices are present in two different regions, residues 98-107 and 114-135, and are connected by a native disulfide bond. The CD spectra of two peptides that correspond to the helical regions are characterized by weak helical signatures, and the sum of their CD spectra is nearly the same as the spectrum of disulfide-reduced CHIBLΔF. Therefore, the non-native helices are stabilized by the disulfide, and non-native helix formation may occur only during the refolding of the disulfide-intact protein. Supporting this conclusion is the observation that tear lipocalin, a homologue of ELG that lacks the disulfide, does not form non-native helices during folding.
机译：标牌β-乳酰叶蛋白（ELG）在重折叠期间和部分折叠状态下假设非天然螺旋。以前，圆形二色性（CD）与位点导向的诱变结合在ELG的酸和冷却状态中鉴定了螺旋区域。还已知ELG，ChiBL（残基88-142）的片段具有与冷的状态类似的结构。对于本文报道的研究，通过CD和核磁共振光谱研究了较短片段的结构ChiblΔF（残基97-142）。所清楚的化学变换清楚地表明，非天然α-螺旋存在于两个不同的区域，残基98-107和114-135中，并通过天然二硫键连接。对应于螺旋区域的两种肽的CD光谱的特征在于弱螺旋签名，并且其CD光谱的总和与二硫化物还原的ChiblΔF的光谱几乎相同。因此，非天然螺旋通过二硫化物稳定，并且仅在二硫化物完整蛋白质的重折叠期间可能仅发生非天然螺旋形成。支持这一结论是观察到泪滴，缺乏二硫化物的ELG同源物，在折叠期间不会形成非天然螺旋。

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  • 来源
    《Biochemistry》 |2011年第49期|共8页
  • 作者

    Mio Yamamoto; Kanako Nakagawa; Kazuo Fujiwara; Akio Shimizu; Mitsunori Ikeguchi; Masamichi Ikeguchi;

  • 作者单位

    Department of Bioinformatics Soka University 1-236 Tangi-cho Hachioji Tokyo 192-8577 Japan;

    Department of Bioinformatics Soka University 1-236 Tangi-cho Hachioji Tokyo 192-8577 Japan;

    Department of Bioinformatics Soka University 1-236 Tangi-cho Hachioji Tokyo 192-8577 Japan;

    Department of Environmental Engineering for Symbiosis Soka University 1-236 Tangi-cho Hachioji Tokyo 192-8577 Japan;

    Department of Supramolecular Biology Graduate School of Nanobioscience Yokohama City University 1-7-29 Suehiro-cho Tsurumi-ku Yokohama 230-0045 Japan;

    Department of Bioinformatics Soka University 1-236 Tangi-cho Hachioji Tokyo 192-8577 Japan;

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  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类 生物化学;
  • 关键词

    Native Disulfide; Helical Structures; β-Lactoglobulin;

    机译：天然二硫化物;螺旋结构;β-乳酰脱蛋白;

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