Ligand Binding in Allosteric Flavoproteins: Part 2. Quantitative Analysis of the Redox-Dependent Interaction of the Apoptosis-Inducing Factor (AIF) with Its Protein Partner
Capitolo
Data di Pubblicazione:
2021
Citazione:
Ligand Binding in Allosteric Flavoproteins: Part 2. Quantitative Analysis of the Redox-Dependent Interaction of the Apoptosis-Inducing Factor (AIF) with Its Protein Partner / P. Cocomazzi, D. Tarantino, E. Mastrangelo, A. Aliverti (METHODS IN MOLECULAR BIOLOGY). - In: Flavins and Flavoproteins / [a cura di] M. Barile. - Prima edizione. - [s.l] : Springer, 2021. - ISBN 9781071612859. - pp. 189-198 [10.1007/978-1-0716-1286-6_12]
Abstract:
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.
Tipologia IRIS:
03 - Contributo in volume
Keywords:
Protein–ligand interaction; Protein–protein interaction; Redox-linked binding; Microscale thermophoresis
Elenco autori:
P. Cocomazzi, D. Tarantino, E. Mastrangelo, A. Aliverti
Link alla scheda completa:
Titolo del libro:
Flavins and Flavoproteins