High-Resolution Cryo-Electron Microscopy Structure Determination of
200 kV
alpha-helical
cryo-EM
detergents
fully embed
membrane protein
structural biology
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
20 Apr 2024
20 Apr 2024
Historique:
received:
29
03
2024
revised:
16
04
2024
accepted:
18
04
2024
medline:
27
4
2024
pubmed:
27
4
2024
entrez:
27
4
2024
Statut:
epublish
Résumé
Membrane proteins constitute about 20% of the human proteome and play crucial roles in cellular functions. However, a complete understanding of their structure and function is limited by their hydrophobic nature, which poses significant challenges in purification and stabilization. Detergents, essential in the isolation process, risk destabilizing or altering the proteins' native conformations, thus affecting stability and functionality. This study leverages single-particle cryo-electron microscopy to elucidate the structural nuances of membrane proteins, focusing on the SLAC1 bacterial homolog from
Identifiants
pubmed: 38674110
pii: ijms25084528
doi: 10.3390/ijms25084528
pii:
doi:
Substances chimiques
Bacterial Proteins
0
Detergents
0
Membrane Proteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM