Comparative cross-linking and mass spectrometry of an intact F-type ATPase suggest a role for phosphorylation

Nature Communications

Volumn 4, Issue , 2013, Pages

  Schmidt, Carla ^a   Zhou, Min ^a   Marriott, Hazel ^a   Morgner, Nina ^a   Politis, Argyris ^a   Robinson, Carol V ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

NUCLEOTIDE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

CHLOROPLAST; ENZYME ACTIVITY; MASS SPECTROMETRY; MEMBRANE; STOICHIOMETRY;

ARTICLE; CHLOROPLAST; COMPARATIVE STUDY; CONFORMATIONAL TRANSITION; ENZYME ISOLATION; ENZYME PHOSPHORYLATION; MASS SPECTROMETRY; NUCLEOTIDE BINDING SITE; PROTEIN CROSS LINKING; SPINACH; STOICHIOMETRY;

CHLOROPLASTS; CROSS-LINKING REAGENTS; ENZYME STABILITY; MASS SPECTROMETRY; NUCLEOTIDES; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN SUBUNITS; PROTON-TRANSLOCATING ATPASES; SPINACIA OLERACEA;

SPINACIA OLERACEA;

EID: 84879967659     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms2985     Document Type: Article

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