等温滴定量热法
化学
等温微量热法
动力学
酶动力学
色谱法
酶
生物化学
活动站点
热力学
物理
量子力学
焓
作者
Robert J. Falconer,Boelo Schuur,Anthony Mittermaier
摘要
Abstract The last 5 years have seen a series of advances in the application of isothermal titration microcalorimetry (ITC) and interpretation of ITC data. ITC has played an invaluable role in understanding multiprotein complex formation including proteolysis‐targeting chimeras (PROTACS), and mitochondrial autophagy receptor Nix interaction with LC3 and GABARAP. It has also helped elucidate complex allosteric communication in protein complexes like trp RNA‐binding attenuation protein (TRAP) complex. Advances in kinetics analysis have enabled the calculation of kinetic rate constants from pre‐existing ITC data sets. Diverse strategies have also been developed to study enzyme kinetics and enzyme‐inhibitor interactions. ITC has also been applied to study small molecule solvent and solute interactions involved in extraction, separation, and purification applications including liquid‐liquid separation and extractive distillation. Diverse applications of ITC have been developed from the analysis of protein instability at different temperatures, determination of enzyme kinetics in suspensions of living cells to the adsorption of uremic toxins from aqueous streams.
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