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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Relationship of Leffler (Bronsted) α values and protein folding Φ values to position of transition-state structures on reaction coordinates
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Relationship of Leffler (Bronsted) α values and protein folding Φ values to position of transition-state structures on reaction coordinates

机译：Leffler（Bronsted）α值和蛋白质折叠Φ值与过渡态结构在反应坐标上的位置的关系

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摘要

The positions of transition states along reaction coordinates (r) for simple chemical reactions are often estimated from Leffler α values, the slope of plots of ΔG (activation energy) versus ΔG~0 (equilibrium free energy) for a series of structural variants. Protein folding is more complex than simple chemical reactions and has a multitude of reaction coordinates. Φ-Value analysis measures degree of structure formation at individual residues in folding transition states from the ratio ΔΔG/ΔΔG~0 for mutations. α values are now being used to analyze protein folding by lumping series of Φ values into single plots. But, there are discrepancies in the values of α for folding with more classical measures of the extent of structure formation, which I rationalize here. I show for chemical reactions with just a single reaction coordinate that α = r only for limiting cases, such as for reactants and products being in parabolic energy wells of identical curvature. Otherwise, α can differ radically from r, with α being determined just by the angles of intersection of reactant and product energy surfaces. Φ is an index of the progress of a local, energy-based reaction coordinate at the global transition state: Φ <0.5 corresponds to <50% progress of the local coordinate at the global transition state and Φ >0.5 means >50%. Protein Leffler plots can force different local indexes to a single fit and give skewed underestimates of the extent of global structure formation in transition states that differ from other measures of structure formation.
机译：对于简单的化学反应，沿反应坐标（r）的过渡态位置通常是根据Lefflerα值，一系列结构变体的ΔG（活化能）与ΔG〜0（平衡自由能）的关系图的斜率估算的。蛋白质折叠比简单的化学反应更复杂，并且具有多个反应坐标。 Φ值分析根据突变的比率ΔΔG/ΔΔG〜0来衡量折叠过渡状态下单个残基的结构形成程度。现在，通过将一系列Φ值集中到单个图中，α值正用于分析蛋白质折叠。但是，折叠的α值与结构形成程度的更为经典的度量之间存在差异，我在这里对此进行合理化说明。对于仅具有单个反应坐标的化学反应，我显示了α= r仅用于有限的情况，例如，对于反应物和产物处于相同曲率的抛物线能量井中。否则，α可能与r截然不同，α仅由反应物和产物能表面的交角决定。 Φ是全局过渡状态下基于局部能量的反应坐标的进度的索引：Φ<0.5对应于全局过渡状态下局部坐标的<50％进度，Φ> 0.5表示> 50％。蛋白质勒夫勒图可以迫使不同的局部指数适应单一拟合，并且偏向低估了与其他结构形成测量方法不同的过渡状态下整体结构形成的程度。

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