Methodological approaches for the analysis of transmembrane domain interactions: A systematic review.
Membrane protein
Methods
Protein folding
Protein-protein interaction
Transmembrane
Journal
Biochimica et biophysica acta. Biomembranes
ISSN: 1879-2642
Titre abrégé: Biochim Biophys Acta Biomembr
Pays: Netherlands
ID NLM: 101731713
Informations de publication
Date de publication:
01 12 2021
01 12 2021
Historique:
received:
30
04
2021
revised:
28
06
2021
accepted:
21
07
2021
pubmed:
1
8
2021
medline:
4
1
2022
entrez:
31
7
2021
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 34331948
pii: S0005-2736(21)00161-9
doi: 10.1016/j.bbamem.2021.183712
pii:
doi:
Substances chimiques
Membrane Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Systematic Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
183712Informations de copyright
Copyright © 2021 Elsevier B.V. All rights reserved.