pH-triggered, activated-state conformations of the influenza hemagglutinin fusion peptide revealed by NMR

Proceedings of the National Academy of Sciences of the United States of America

Volumn 109, Issue 49, 2012, Pages 19994-19999

  Lorieau, Justin L ^a   Louis, John M ^a   Schwieters, Charles D ^b   Bax, Adriaan ^a  

^a NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

^b NATIONAL INSTITUTES OF HEALTH   (United States)

Author keywords

Conformational ensemble; Dynamics; Membrane proteins; RDC; Relaxation dispersion

Indexed keywords

HYBRID PROTEIN; INFLUENZA VIRUS HEMAGGLUTININ;

ARTICLE; DNA HAIRPIN; GENE MUTATION; MEMBRANE FUSION; NUCLEAR OVERHAUSER EFFECT; PH; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STRUCTURE; WILD TYPE;

AMINO ACID SEQUENCE; HEMAGGLUTININS, VIRAL; HYDROGEN-ION CONCENTRATION; MEMBRANE FUSION; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; VIRUS INTERNALIZATION;

EID: 84870604188     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1213801109     Document Type: Article

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