6533b829fe1ef96bd128a41b

RESEARCH PRODUCT

Methodological approaches for the analysis of transmembrane domain interactions: A systematic review

Brayan GrauLuis Martínez-gilIsmael MingarroGerard Duart

subject

Protein FoldingBacteriaChemistryIn silicoProtein domainBiophysicsMembrane ProteinsCell CommunicationCell BiologyComputational biologyBiochemistryTransmembrane proteinIn vitroProtein–protein interactionTransmembrane domainProtein DomainsMembrane proteinProtein foldingProtein Interaction MapsHydrophobic and Hydrophilic Interactions

description

The study of protein-protein interactions (PPI) has proven fundamental for the understanding of the most relevant cell processes. Any protein domain can participate in PPI, including transmembrane (TM) segments that can establish interactions with other TM domains (TMDs). However, the hydrophobic nature of TMDs and the environment they occupy complicates the study of intramembrane PPI, which demands the use of specific approaches and techniques. In this review, we will explore some of the strategies available to study intramembrane PPI in vitro, in vivo, and, in silico, focusing on those techniques that could be carried out in a standard molecular biology laboratory regarding its previous experience with membrane proteins.

yearjournalcountryeditionlanguage
2021-12-01Biochimica et Biophysica Acta (BBA) - Biomembranes
https://doi.org/10.1016/j.bbamem.2021.183712