Domain Features of the Peripheral Stalk Subunit H of the Methanogenic A1AO ATP Synthase and the NMR Solution Structure of H1-47
Author:
Publisher
Elsevier BV
Subject
Biophysics
Reference42 articles.
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3. The relationship of A1AO ATPsynthases and V1VO ATPases: structural, functional and mechanistical aspects of an energy producer and an energy transducer;Grüber;Bioessays,2008
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1. The Critical Roles of Residues P235 and F236 of Subunit A of the Motor Protein A-ATP Synthase in P-Loop Formation and Nucleotide Binding;Journal of Molecular Biology;2010-09
2. Crystal and solution structure of the C-terminal part of the Methanocaldococcus jannaschii A1AO ATP synthase subunit E revealed by X-ray diffraction and small-angle X-ray scattering;Journal of Bioenergetics and Biomembranes;2010-06-23
3. Purification and crystallization of the entire recombinant subunit E of the energy producer A1AoATP synthase;Acta Crystallographica Section F Structural Biology and Crystallization Communications;2010-02-25
4. Disulfide linkage in the coiled-coil domain of subunit H of A1 AO ATP synthase from Methanocaldococcus jannaschii and the NMR structure of the C-terminal segment H85-104;FEBS Letters;2009-12-22
5. Solution Structure, Determined by Nuclear Magnetic Resonance, of the b30-82 Domain of Subunit b of Escherichia coli F 1 F o ATP Synthase;Journal of Bacteriology;2009-12-15
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