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Energetics-Based Methods for Protein Folding and Stability Measurements

机译：基于能量学的蛋白质折叠和稳定性测量方法

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摘要

Over the past 15 years, a series of energetics-based techniques have been developed for the thermodynamic analysis of protein folding and stability. These techniques include Stability of Unpurified Proteins from Rates of amide H/D Exchange (SUPREX), pulse proteolysis, Stability of Proteins from Rates of Oxidation (SPROX), slow histidine H/D exchange, lysine amidination, and quantitative cysteine reactivity (QCR). The above techniques, which are the subject of this review, all utilize chemical or enzymatic modification reactions to probe the chemical denaturant-or temperature-induced equilibrium unfolding properties of proteins and protein-ligand complexes. They employ various mass spectrometry-, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE)-, and optical spectroscopy-based readouts that are particularly advantageous for high-throughput and in some cases multiplexed analyses. This has created the opportunity to use protein folding and stability measurements in new applications such as in high-throughput screening projects to identify novel protein ligands and in mode-of-action studies to identify protein targets of a particular ligand.
机译：在过去的15年中，已经开发出了一系列基于能量学的技术来对蛋白质折叠和稳定性进行热力学分析。这些技术包括来自酰胺H / D交换速率（SUPREX）的未纯化蛋白的稳定性，脉冲蛋白水解，来自氧化率（SPROX）的蛋白稳定性，组氨酸H / D交换慢，赖氨酸酰胺化和定量半胱氨酸反应性（QCR） 。作为本综述主题的上述技术均利用化学或酶促修饰反应来探测蛋白质和蛋白质-配体复合物的化学变性或温度诱导的平衡展开特性。他们采用各种质谱分析，十二烷基硫酸钠-聚丙烯酰胺凝胶电泳（SDS-PAGE）和基于光谱的读数，这些读数对于高通量和某些情况下的多重分析特别有利。这创造了在新应用中使用蛋白质折叠和稳定性测量的机会，例如在高通量筛选项目中鉴定新的蛋白质配体，在作用方式研究中鉴定特定配体的蛋白质靶标。

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