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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Multiple subsets of side-chain packing in partially folded states of alpha-lactalbumins
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Multiple subsets of side-chain packing in partially folded states of alpha-lactalbumins

机译：α-乳清蛋白部分折叠状态下侧链堆积的多个子集

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摘要

Photochemically induced dynamic nuclear polarization NMR pulse-labeling techniques have been used to obtain detailed information about side-chain surface accessibilities in the partially folded (molten globule) states of bovine and human a-lactalbumin prepared under a variety of well defined conditions. Pulse labeling involves generating nuclear polarization in the partially folded state, rapidly refolding the protein within the NMR sample tube, then detecting the polarization in the well dispersed native-state Spectrum. Differences in the solvent accessibility of specific side chains in the various molten globule states indicate that the hydrophobic clusters involved in stabilizing the a-lactalbumin fold can be formed from interactions between a variety of different hydrophobic residues in both native and nonnative environments. The multiple subsets of hydrophobic clusters are likely to result from the existence of distinct but closely related local minima on the free-energy landscape of the protein and show that the fold and topology of a given protein may be formed from degenerate groups of side chains.
机译：已使用光化学诱导的动态核极化NMR脉冲标记技术来获得有关在各种明确定义的条件下制备的牛和人α-乳清蛋白的部分折叠（熔融小球）状态下侧链表面可及性的详细信息。脉冲标记包括在部分折叠状态下产生核极化，在NMR样品管中快速重新折叠蛋白质，然后在分散良好的原始光谱中检测极化。在各种熔融小球状态下，特定侧链在溶剂可及性上的差异表明，稳定α-乳白蛋白折叠所涉及的疏水簇可以由天然和非天然环境中各种不同疏水残基之间的相互作用形成。疏水簇的多个子集很可能是由于蛋白质自由能图谱上存在独特但密切相关的局部极小值所致，并表明给定蛋白质的折叠和拓扑可能是由简并的侧链基团形成的。

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