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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Probing site-specific conformational distributions in protein folding with solid-state NMR
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Probing site-specific conformational distributions in protein folding with solid-state NMR

机译：用固态NMR探测蛋白质折叠中的位点特异性构象分布

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摘要

We demonstrate an experimental approach to structural studies of unfolded and partially folded proteins in which conformational distributions are probed at a site-specific level by 2D solid-state ~(13)C NMR spectroscopy of glassy frozen solutions. Experiments on chemical denaturation of the 35-residue villin headpiece subdo-main, a model three-helix-bundle protein with a known folded structure, reveal that ~(13)C-labeled residues in the three helical segments of the folded state have markedly different conformational distributions in the unfolded state. Moreover, the 2D solid-state NMR line shapes near the unfolding midpoint do not fit a simple two-state model, in which the conformational distributions of the unfolded component are assumed to be independent of denaturant concentration. Comparison with solid-state NMR spectra of peptides containing the individual helical segments suggests an alternative two-step description of conformational distributions in partially folded states of the helical villin headpiece subdomain, in which chemical denaturation is viewed as a disruption of tertiary contacts followed by equilibration of local secondary structure according to the intrinsic helical propensities of individual segments.
机译：我们展示了一种结构展开和部分折叠的蛋白质的结构研究的实验方法，其中构象分布是通过玻璃态冷冻溶液的2D固态〜（13）C NMR光谱在位点特异性水平上探测到的。对具有残留折叠结构的模型三螺旋束蛋白35残基的villin头部件次主体进行化学变性的实验表明，折叠状态的三个螺旋段中〜（13）C标记的残基具有明显的展开状态下的不同构象分布。此外，在展开中点附近的2D固态NMR线形不适合简单的两态模型，在该模型中，未展开成分的构象分布被认为与变性剂浓度无关。与包含单个螺旋段的肽段的固态NMR光谱比较表明，螺旋式villin头亚结构域的部分折叠状态的构象分布的另一步描述为两步，其中化学变性被认为是三级接触的破坏，然后是平衡根据各个段的固有螺旋倾向确定局部二级结构。

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