Backbone and methyl assignment of bacteriorhodopsin incorporated into nanodiscs.
Membrane protein
Nanodisc
Resonance assignment
Solution-state NMR
Journal
Journal of biomolecular NMR
ISSN: 1573-5001
Titre abrégé: J Biomol NMR
Pays: Netherlands
ID NLM: 9110829
Informations de publication
Date de publication:
Jan 2020
Jan 2020
Historique:
received:
10
09
2019
accepted:
11
11
2019
pubmed:
23
11
2019
medline:
10
10
2020
entrez:
23
11
2019
Statut:
ppublish
Résumé
Resonance assignments are challenging for membrane proteins due to the size of the lipid/detergent-protein complex and the presence of line-broadening from conformational exchange. As a consequence, many correlations are missing in the triple-resonance NMR experiments typically used for assignments. Herein, we present an approach in which correlations from these solution-state NMR experiments are supplemented by data from
Identifiants
pubmed: 31754899
doi: 10.1007/s10858-019-00289-7
pii: 10.1007/s10858-019-00289-7
pmc: PMC7015963
doi:
Substances chimiques
Bacteriorhodopsins
53026-44-1
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
45-60Subventions
Organisme : Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung
ID : Grant No 310030_159453
Organisme : Forschungskredit der Universität Zürich
ID : FK-18-083
Organisme : INEXT
ID : 653706
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