Nucleotide binding to active and 4-chloro-7-nitrobenzofurazan-inhibited forms of chloroplast F1-ATPase — an NMR study
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Biochemistry,Biophysics
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1. Catalytic Sites of F1-ATPase from Escherichia coli was Investigated with GTP and GDP Titration Using31P NMR Spectroscopy;Bulletin of the Korean Chemical Society;2012-07-20
2. Conformational Changes of Nucleotide Binding Sites Following Sequential Addition of ADP to Nucleotide-depleted F1-ATPase of Escherichia coli Investigated with31P NMR Spectroscopy;Bulletin of the Korean Chemical Society;2011-03-20
3. Observation of Asymmetry amongst Nucleotide Binding Sites of F1-ATPase of Escherichia coli by31P NMR Spectroscopy;Bulletin of the Korean Chemical Society;2011-02-20
4. 31P NMR Spectroscopy Revealed Adenylate kinase-like Activity and Phosphotransferase-like Activity from F1-ATPase of Escherichia coli;Bulletin of the Korean Chemical Society;2011-01-20
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