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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Correlated dynamics of consecutive residues reveal transient and cooperative unfolding of secondary structure in proteins.
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Correlated dynamics of consecutive residues reveal transient and cooperative unfolding of secondary structure in proteins.

机译：连续残基的相关动力学揭示了蛋白质二级结构的瞬时和协同展开。

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摘要

Nuclear spin relaxation is a powerful method for studying molecular dynamics at atomic resolution. Recent methods development in biomolecular NMR spectroscopy has enabled detailed investigations of molecular dynamics that are critical for biological function, with prominent examples addressing allostery, enzyme catalysis, and protein folding. Dynamic processes with similar correlation times are often detected in multiple locations of the molecule, raising the question of whether the underlying motions are correlated (corresponding to concerted fluctuations involving many atoms distributed across extended regions of the molecule) or uncorrelated (corresponding to independent fluctuations involving few atoms in localized regions). Here, we have used (13)C(alpha)(i - 1)/(13)C(alpha)(i) differential multiple-quantum spin relaxation to provide direct evidence for correlated dynamics of consecutive amino acid residues in the protein sequence. By monitoring overlapping pairs of residues (i - 1 and i, i and i + 1, etc.), we identified correlated motions that extend through continuous segments of the sequence. We detected significant correlated conformational transitions in the native state of the E140Q mutant of the calmodulin C-terminal domain. Previous work has shown that this domain exchanges between two major conformational states that resemble the functionally relevant open and closed states of the WT protein, with a mean correlation time of approximately 20 micros. The present results reveal that an entire alpha-helix undergoes partial unraveling in a transient and cooperative manner.
机译：核自旋弛豫是研究原子分辨率下的分子动力学的有力方法。生物分子NMR光谱学的最新方法开发已使对生物学功能至关重要的分子动力学的详细研究成为可能，其中最重要的例子涉及变构，酶催化和蛋白质折叠。通常会在分子的多个位置检测到具有相似相关时间的动态过程，这引发了以下问题：基本运动是相关的（对应于涉及分布在分子扩展区域的许多原子的协调波动）还是不相关的（对应于涉及局部区域中的原子很少）。在这里，我们已经使用（13）Cα（i-1）/（13）Cα（i）微分多量子自旋弛豫来提供蛋白质序列中连续氨基酸残基的相关动力学的直接证据。 。通过监视重叠的残基对（i-1和i，i和i + 1等），我们确定了相关运动，这些运动延伸到序列的连续片段。我们在钙调蛋白C末端域的E140Q突变体的天然状态下检测到显着相关的构象转变。先前的研究表明，该结构域在两个主要构象状态之间进行交换，这两个状态类似于WT蛋白的功能相关打开和关闭状态，平均相关时间约为20微米。目前的结果表明，整个α-螺旋以瞬时和协作的方式经历了部分分解。

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