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首页> 外文期刊>Biochemistry >Consequences of Single-Site Mutations in the Intestinal Fatty Acid Binding Protein
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Consequences of Single-Site Mutations in the Intestinal Fatty Acid Binding Protein

机译:肠道脂肪酸结合蛋白中单位点突变的后果

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摘要

The intestinal fatty acid binding protein(IFABP) is a small (15kDa) protein consisting mostly of 10 antiparallel beta-strands(A-J) and a small helical region that serves as a portal for the ligand.Two beta-sheet structures (strands A-E adn F-J) surround a cavity into which the ligand binds.In this work,we investigated how changes in the side chanis of specific residues are propagated through the strcuture.To determine what these changes were and how they relate to changes in stability,~14N chemicla shift perturbations were measured and compared to those of the wild-type protein.Seven mutations,five of which change either valine or leucine toglycine,have been examined.all these mutants were less stable than wild-type IFABP,suggesting some structural changes.For five of the mutants,the data suggest that destabilization of a small region of the protein propagates throughout the structure,resulting in an overall denaturation curves suggests that th edestabilization ofone region may not be transmitted to other regions in a cooperative manner.It is shown that the effect of mutating hydrophobic residues is much greater than that observed upon mutation of a solvent-exposed polar residue.
机译:肠脂肪酸结合蛋白(IFABP)是一种小的(15kDa)蛋白,主要由10条反平行的β-链(AJ)和一个小的螺旋区域组成,该螺旋区域充当配体的门户。两个β-折叠结构(链AE和FJ)围绕着一个与配体结合的空腔。在这项工作中,我们研究了特定残基侧链的变化如何通过结构传播。为了确定这些变化是什么以及它们与稳定性的变化之间的关系,〜14N化学测量了位移扰动并将其与野生型蛋白的扰动进行了比较。已检查了七个突变,其中五个突变为缬氨酸或亮氨酸至甘氨酸。所有这些突变体均不如野生型IFABP稳定,表明存在一些结构变化。在5个突变体中,数据表明该蛋白小区域的失稳在整个结构中扩散,导致整体变性曲线表明,可能没有一个区域的稳定。结果表明,疏水残基突变的效果远大于暴露于溶剂的极性残基突变后的效果。

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