Pica Andrea, Graziano Giuseppe
Dipartimento di Scienze Chimiche, Università degli Studi di Napoli Federico II, Complesso Universitario di Monte Sant'Angelo, Via Cintia, Napoli, 80126, Italy.
Dipartimento di Scienze e Tecnologie, Università del Sannio, Via Port'Arsa 11, Benevento, 82100, Italy.
Biopolymers. 2016 Dec;105(12):856-63. doi: 10.1002/bip.22923.
An entropic stabilization mechanism has recently gained attention and credibility as the physical ground for the extra thermal stability of globular proteins from thermophilic microorganisms. An empirical result, obtained from the analysis of thermodynamic data for a large set of proteins, strengthens the general reliability of the theoretical approach originally devised to rationalize the occurrence of cold denaturation [Graziano, PCCP 2014, 16, 21755-21767]. It is shown that this theoretical approach can readily account for the entropic stabilization mechanism. On decreasing the conformational entropy gain associated with denaturation, the thermal stability of a model globular protein increases markedly.
作为嗜热微生物球状蛋白质具有额外热稳定性的物理基础，一种熵稳定机制最近受到关注并具有可信度。从大量蛋白质的热力学数据分析中得到的一个实证结果，加强了最初为解释冷变性现象而设计的理论方法的总体可靠性[格拉齐亚诺，《物理化学化学物理》2014年，第16卷，21755 - 21767页]。结果表明，这种理论方法能够很容易地解释熵稳定机制。随着与变性相关的构象熵增加量的减少，一种模型球状蛋白质的热稳定性显著提高。
