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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >THERMODYNAMICS OF AMINO ACID SIDE-CHAIN INTERNAL ROTATIONS
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THERMODYNAMICS OF AMINO ACID SIDE-CHAIN INTERNAL ROTATIONS

机译：氨基酸侧链内部旋转的热力学

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The absolute Gibbs energy, enthalpy and entropy of each of the internal rotations found in protein side chains has been calculated. The calculation requires the moments of inertia of the side chains about each bond, the potential energy barrier and the symmetry number and gives the maximum possible thermodynamic consequences of restricting side chain motion when a protein folds. Hindering side chain internal rotations is unfavourable in terms of Gibbs energy and entropy; it is enthalpically favourable at 0K. At room temperature, it is estimated that the adverse entropy of hindering buried side chain internal rotation is only 25% of the absolute entropy. The difference between absolute entropies in the folded and unfolded states gives the entropy change for folding. The estimated Gibbs energy change for restricting each residue correlates moderately well with the probability of that residue being found on the folded protein surface, rather than in the protein interior (where motion is restricted). [References: 33]
机译：已计算出蛋白质侧链中每个内旋的绝对吉布斯能量，焓和熵。计算需要侧链围绕每个键的惯性矩，势能垒和对称数，并给出蛋白质折叠时限制侧链运动的最大可能的热力学后果。就吉布斯能量和熵而言，阻碍侧链内部旋转是不利的。在0K时，它在焓上是有利的。在室温下，据估计阻碍掩埋侧链内部旋转的逆熵仅为绝对熵的25％。折叠状态和展开状态下的绝对熵之差给出了折叠的熵变化。估计的用于限制每个残基的吉布斯能量变化与在折叠的蛋白质表面而不是在蛋白质内部（运动受限制的位置）发现该残基的可能性有中等程度的相关性。 [参考：33]

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