Ligand Binding in Allosteric Flavoproteins: Part 2. Quantitative Analysis of the Redox-Dependent Interaction of the Apoptosis-Inducing Factor (AIF) with Its Protein Partner
| Autor: | Delia Tarantino, Paolo Cocomazzi, Alessandro Aliverti, Eloise Mastrangelo |
|---|---|
| Rok vydání: | 2021 |
| Předmět: |
0303 health sciences
biology Chemistry Microscale thermophoresis 030302 biochemistry & molecular biology Allosteric regulation Flavoprotein Flavin group Cofactor Protein–protein interaction 03 medical and health sciences biology.protein Biophysics Apoptosis-inducing factor Quantitative analysis (chemistry) 030304 developmental biology |
| Zdroj: | Methods in Molecular Biology ISBN: 9781071612859 |
| DOI: | 10.1007/978-1-0716-1286-6_12 |
| Popis: | To perform their action usually flavoproteins interact transiently with a variety of molecular partners, whose binding is reciprocally affected and often controlled by the redox state of the bound flavin cofactor. As a case study, here we describe an approach for the quantitative characterization of the redox-controlled interaction of the mammalian apoptosis inducing factor (AIF) with one of its known protein partners, namely, the mitochondrial coiled-coil-helix-coiled-coil-helix domain-containing protein 4 (CHCHD4). In particular, we report a protocol for the titration of the flavoprotein in both in its oxidized and reduced states with CHCHD4, using an implementation of the MicroScale Thermophoresis (MST) technique. |
| Databáze: | OpenAIRE |
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