Utilizing Thermal Shift Assay to Probe Substrate Binding to Selenoprotein O.

ABSTRACT: Defining the biological importance of proteins with unknown functions poses a significant obstacle in understanding cellular processes. Although bioinformatic and structural predictions have contributed to the study of unknown proteins, in vitro experimental validations are often hampered by the optimal conditions and cofactors required for biochemical activity. Cofactor binding is not only essential for the activity of some enzymes but may also enhance the thermal stability of the protein. One practical application of this phenomenon lies in utilizing the change in thermal stability, as measured by alterations in the protein's melting temperature, to probe ligand binding. Thermal shift assay (TSA) can be used to analyze the binding of different ligands to the protein of interest or find a

SUBMITTER: Gonzalez A 

PROVIDER: S-EPMC11608410 | biostudies-literature | 2024 Aug

REPOSITORIES: biostudies-literature