Thermott: A comprehensive online tool for protein-ligand binding constant determination

被引：25

作者：

Gedgaudas, Marius ^{[1
]}

Baronas, Denis ^{[1
]}

Kazlauskas, Egidijus ^{[1
]}

Petrauskas, Vytautas ^{[1
]}

Matulis, Daumantas ^{[1
]}

机构：

[1] Vilnius Univ, Inst Biotechnol, Life Sci Ctr, Dept Biothermodynam & Drug Design, Sauletekio 7, LT-10257 Vilnius, Lithuania

来源：

DRUG DISCOVERY TODAY | 2022年 / 27卷 / 08期

关键词：

Thermal shift assay; Differential scanning calorimetry; Enthalpy; Protein unfolding; Protein-ligand binding; SHIFT ASSAYS;

D O I：

10.1016/j.drudis.2022.05.008

中图分类号：

R9 [药学];

学科分类号：

1007 ;

摘要：

The thermal shift assay is one of the most universal techniques to determine protein-ligand affinities ranging from millimolar to picomolar levels in a single ligand dosing experiment. However, the complexity of thermodynamic data analysis leads to an underuse of this technique. We have developed a user-friendly, open-source, free online analysis software to study any protein-ligand interaction thermal shift data and yield a comprehensive thermodynamic characterization of the binding reaction.

引用

收藏

页码：2076 / 2079

页数：4

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