Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, USA.
Protein Sci. 2024 Jun;33(6):e5013. doi: 10.1002/pro.5013.
Many small globular proteins exist in only two states-the physiologically relevant folded state and an inactive unfolded state. The active state is stabilized by numerous weak attractive contacts, including hydrogen bonds, other polar interactions, and the hydrophobic effect. Knowledge of these interactions is key to understanding the fundamental equilibrium thermodynamics of protein folding and stability. We focus on one such interaction, that between amide and aromatic groups. We provide a statistically convincing case for quantitative, linear entropy-enthalpy compensation in forming aromatic-amide interactions using published model compound transfer-free energy data.
许多小的球状蛋白质只存在两种状态——生理相关的折叠状态和非活性的展开状态。活性状态由许多弱的吸引力接触稳定，包括氢键、其他极性相互作用和疏水效应。这些相互作用的知识是理解蛋白质折叠和稳定性基本平衡热力学的关键。我们关注的是其中一种相互作用，即酰胺和芳基之间的相互作用。我们使用已发表的模型化合物转移自由能数据，提供了一个具有统计学说服力的案例，证明了形成芳基-酰胺相互作用的定量线性熵-焓补偿。
