Determination of Protein-Ligand Binding Affinities by Thermal Shift Assay.

ABSTRACT: Quantification of protein-ligand interactions is crucial for understanding the protein's biological function and for drug discovery. In this study, we employed three distinct approaches for determination of protein-ligand binding affinities by a thermal shift assay using a single ligand concentration. We present the results of the comparison of the performance of the conventional curve fitting (CF) method and two newly introduced methods - assuming zero heat capacity change across small temperature ranges (ZHC) and utilizing the unfolding equilibrium constant (UEC); the latter has the advantage of reducing calculations by obtaining the unfolding equilibrium constant directly from the experimental data. Our results highlight superior performance of the ZHC and UEC methods over the conventio

SUBMITTER: Khan MF 

PROVIDER: S-EPMC11487536 | biostudies-literature | 2024 Oct

REPOSITORIES: biostudies-literature