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

Biochim Biophys Acta Biomembr. 2021 Dec 1;1863(12):183712. doi: 10.1016/j.bbamem.2021.183712. Epub 2021 Jul 28.

Abstract

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.

Keywords: Membrane protein; Methods; Protein folding; Protein-protein interaction; Transmembrane.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review
  • Systematic Review

MeSH terms

  • Bacteria / genetics
  • Cell Communication / genetics
  • Hydrophobic and Hydrophilic Interactions
  • Membrane Proteins / chemistry
  • Membrane Proteins / genetics*
  • Protein Domains / genetics*
  • Protein Folding
  • Protein Interaction Maps / genetics*

Substances

  • Membrane Proteins