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用于研究蛋白质-配体相互作用的等温滴定量热法。

Isothermal titration calorimetry for studying protein-ligand interactions.

作者信息

Damian Luminita

机构信息

Microcal Products, GE Healthcare, Little Chalfont, UK.

出版信息

Methods Mol Biol. 2013;1008:103-18. doi: 10.1007/978-1-62703-398-5_4.

DOI:10.1007/978-1-62703-398-5_4
PMID:23729250
Abstract

Isothermal titration calorimetry (ITC) is a biophysical technique that allows a thermodynamic characterization of an interactive system. It is a free in solution technique that requires no labeling, using heat as signal. ITC allows simultaneous determination of affinity K a, stoichiometry n, enthalpy change ΔH and calculation of free energy change ΔG and entropy change ΔS in one single experiment. It is the only technique that allows direct enthalpy change measurement. By accessing the enthalpy change, we get a step closer in estimating the driving forces that characterize the interaction of a protein with a ligand, information much needed in the drug discovery process.

摘要

等温滴定量热法(ITC)是一种生物物理技术,可对相互作用系统进行热力学表征。它是一种无需标记的溶液内技术,以热作为信号。ITC能够在单次实验中同时测定亲和力K a、化学计量数n、焓变ΔH,并计算自由能变ΔG和熵变ΔS。它是唯一能够直接测量焓变的技术。通过获取焓变,我们在估算表征蛋白质与配体相互作用的驱动力方面又迈进了一步,而这正是药物研发过程中急需的信息。

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