Structural Asymmetry and Kinetic Limping of Single Rotary F-ATP Synthases.
Actins
/ chemistry
Adenosine Triphosphate
/ chemistry
Escherichia coli Proteins
/ chemistry
Gold
Kinetics
Models, Molecular
Molecular Conformation
Molecular Structure
Nanotubes
/ chemistry
Protein Binding
Protein Interaction Domains and Motifs
Proton-Translocating ATPases
/ chemistry
Structure-Activity Relationship
Escherichia coli
FOF1 ATP synthase
cryo-EM structure
elasticity
single-molecule fluorescence
subunit rotation
symmetry
Journal
Molecules (Basel, Switzerland)
ISSN: 1420-3049
Titre abrégé: Molecules
Pays: Switzerland
ID NLM: 100964009
Informations de publication
Date de publication:
30 Jan 2019
30 Jan 2019
Historique:
received:
13
12
2018
revised:
23
01
2019
accepted:
29
01
2019
entrez:
2
2
2019
pubmed:
2
2
2019
medline:
21
5
2019
Statut:
epublish
Résumé
F-ATP synthases use proton flow through the F
Identifiants
pubmed: 30704145
pii: molecules24030504
doi: 10.3390/molecules24030504
pmc: PMC6384691
pii:
doi:
Substances chimiques
Actins
0
Escherichia coli Proteins
0
Gold
7440-57-5
Adenosine Triphosphate
8L70Q75FXE
Proton-Translocating ATPases
EC 3.6.3.14
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM050202
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM097510
Pays : United States
Organisme : NIH HHS
ID : R01 GM097510
Pays : United States
Déclaration de conflit d'intérêts
The authors declare no conflict of interest.
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