The conformational landscape of fold-switcher KaiB is tuned to the circadian rhythm timescale.
circadian rhythm
metamorphic protein
relaxation dispersion NMR
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:
05 Nov 2024
05 Nov 2024
Historique:
medline:
31
10
2024
pubmed:
30
10
2024
entrez:
30
10
2024
Statut:
ppublish
Résumé
How can a single protein domain encode a conformational landscape with multiple stably folded states, and how do those states interconvert? Here, we use real-time and relaxation-dispersion NMR to characterize the conformational landscape of the circadian rhythm protein KaiB from
Identifiants
pubmed: 39475637
doi: 10.1073/pnas.2412293121
doi:
Substances chimiques
Bacterial Proteins
0
Circadian Rhythm Signaling Peptides and Proteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
e2412293121Déclaration de conflit d'intérêts
Competing interests statement:D.K. is a co-founder of Relay Therapeutics and MOMA Therapeutics. The remaining authors declare no competing interests.