A thermodynamic analysis of CLC transporter dimerization in lipid bilayers.
CLC
dimerization
heat capacity
membrane
van ‘t Hoff
Journal
Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876
Informations de publication
Date de publication:
10 10 2023
10 10 2023
Historique:
pmc-release:
03
04
2024
medline:
5
10
2023
pubmed:
3
10
2023
entrez:
3
10
2023
Statut:
ppublish
Résumé
The CLC-ec1 chloride/proton antiporter is a membrane-embedded homodimer with subunits that can dissociate and associate, but the thermodynamic driving forces favor the assembled dimer at biological densities. Yet, the physical reasons for this stability are confounding as dimerization occurs via the burial of hydrophobic interfaces away from the lipid solvent. For binding of nonpolar surfaces in aqueous solution, the driving force is often attributed to the hydrophobic effect, but this should not apply in the membrane since there is very little water. To investigate this further, we quantified the thermodynamic changes associated with CLC dimerization in membranes by carrying out a van 't Hoff analysis of the temperature dependency of the free energy of dimerization, Δ
Identifiants
pubmed: 37788312
doi: 10.1073/pnas.2305100120
pmc: PMC10576108
doi:
Substances chimiques
Lipid Bilayers
0
Membrane Transport Proteins
0
Solvents
0
CLC-ec1 protein, E coli
0
Antiporters
0
Escherichia coli Proteins
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
e2305100120Commentaires et corrections
Type : UpdateOf
Type : CommentIn
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