化学
焓
质谱法
电喷雾电离
原籍国
热化学
蛋白质折叠
吉布斯自由能
构象异构
蛋白质-蛋白质相互作用
分子
结晶学
生物物理学
热力学
物理化学
生物化学
色谱法
有机化学
物理
生物
作者
Arthur Laganowsky,David E. Clemmer,David H. Russell
标识
DOI:10.1146/annurev-biophys-102221-101121
摘要
The structures and conformational dynamics of proteins, protein complexes, and their noncovalent interactions with other molecules are controlled specifically by the Gibbs free energy (entropy and enthalpy) of the system. For some organisms, temperature is highly regulated, but the majority of biophysical studies are carried out at room, nonphysiological temperature. In this review, we describe variable-temperature electrospray ionization (vT-ESI) mass spectrometry (MS)-based studies with unparalleled sensitivity, dynamic range, and selectivity for studies of both cold- and heat-induced chemical processes. Such studies provide direct determinations of stabilities, reactivities, and thermodynamic measurements for native and non-native structures of proteins and protein complexes and for protein-ligand interactions. Highlighted in this review are vT-ESI-MS studies that reveal 40 different conformers of chymotrypsin inhibitor 2, a classic two-state (native → unfolded) unfolder, and thermochemistry for a model membrane protein system binding lipid and its regulatory protein.
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