蛋白质折叠中的侧链构象熵。
Side-chain conformational entropy in protein folding.
作者信息
Doig A J, Sternberg M J
机构信息
Department of Biochemistry and Applied Molecular Biology, University of Manchester Institute of Science and Technology, United Kingdom.
出版信息
Protein Sci. 1995 Nov;4(11):2247-51. doi: 10.1002/pro.5560041101.
Abstract
An important, but often neglected, contribution to the thermodynamics of protein folding is the loss of entropy that results from restricting the number of accessible side-chain conformers in the native structure. Conformational entropy changes can be found by comparing the number of accessible rotamers in the unfolded and folded states, or by estimating fusion entropies. Comparison of several sets of results using different techniques shows that the mean conformational free energy change (T delta S) is 1 kcal.mol-1 per side chain or 0.5 kcal.mol-1 per bond. Changes in vibrational entropy appear to be negligible compared to the entropy change resulting from the loss of accessible rotamers. Side-chain entropies can help rationalize alpha-helix propensities, predict protein/inhibitor complex structures, and account for the distribution of side chains on the protein surface or interior.
摘要
对蛋白质折叠热力学有重要贡献但常被忽视的一点是，由于天然结构中可及侧链构象体数量受限而导致的熵损失。构象熵的变化可以通过比较未折叠态和折叠态中可及旋转异构体的数量，或者通过估算融合熵来确定。使用不同技术对几组结果进行比较表明，平均构象自由能变化（TΔS）为每条侧链1千卡·摩尔⁻¹或每个键0.5千卡·摩尔⁻¹。与因可及旋转异构体丧失而导致的熵变相比，振动熵的变化似乎可以忽略不计。侧链熵有助于解释α螺旋倾向、预测蛋白质/抑制剂复合物结构，并说明蛋白质表面或内部侧链的分布情况。
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