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Structure analysis of membrane-reconstituted subunit c-ring of E. coli H+-ATP synthase by solid-state NMR

লেখক

Hideo Akutsu

এতে প্রকাশিত: Journal of Biomolecular NMR

তারিখে প্রকাশিত: 2010-07-02

ভাষা: ইংরেজি ভাষা

মূল বিষয়: এশেরিকিয়া কোলাই

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তারিখ

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Structure of the c14 Rotor Ring of the Proton Translocating Chloroplast ATP Synthase
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High-resolution structure of the rotor ring of a proton-dependent ATP synthase

Özkan Yıldız, Denys Pogoryelov
2008-02-29

Fluid mechanical matching of H+-ATP synthase subunit c-ring with lipid membranes revealed by 2H solid-state NMR.
2008-09-11

Structural interactions between transmembrane helices 4 and 5 of subunit a and the subunit c ring of Escherichia coli ATP synthase
2006-05-19

Structure of tightly membrane-bound mastoparan-X, a G-protein-activating peptide, determined by solid-state NMR

Hideo Akutsu
2006-01-25

A new solution structure of ATP synthase subunit c from thermophilic Bacillus PS3, suggesting a local conformational change for H+-translocation
2006-08-01

Detection of peptide-phospholipid interaction sites in bilayer membranes by 13C NMR spectroscopy: observation of 2H/31P-selective 1H-depolarization under magic-angle spinning

Hideo Akutsu
2006-11-02

Signal assignment and secondary structure analysis of a uniformly [13C, 15N]-labeled membrane protein, H +-ATP synthase subunit c, by magic-angle spinning solid-state NMR.

Hideo Akutsu
2006-03

Catalytic and mechanical cycles in F-ATP synthases. Fourth in the Cycles Review Series

Christoph von Ballmoos, Peter Dimroth
2005-03-31

Structure of the rotor of the V-Type Na+-ATPase from Enterococcus hirae

Takeshi Murata
2005-04-01

Structure of the rotor ring of F-Type Na+-ATPase from Ilyobacter tartaricus.
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UCSF Chimera--a visualization system for exploratory research and analysis

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Signal assignments and chemical-shift structural analysis of uniformly 13C, 15N-labeled peptide, mastoparan-X, by multidimensional solid-state NMR under magic-angle spinning

Hideo Akutsu
2003-01

The Xplor-NIH NMR molecular structure determination package

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Solid-state NMR reveals structural changes in phospholamban accompanying the functional regulation of Ca2+-ATPase
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A graph-theory algorithm for rapid protein side-chain prediction

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Transmembrane interactions in the activation of the Neu receptor tyrosine kinase
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F(0) of ATP synthase is a rotary proton channel. Obligatory coupling of proton translocation with rotation of c-subunit ring
2002-10-01

Structural model of the transmembrane Fo rotary sector of H+-transporting ATP synthase derived by solution NMR and intersubunit cross-linking in situ
2001-07-03

Energy-driven subunit rotation at the interface between subunit a and the c oligomer in the F(O) sector of Escherichia coli ATP synthase
2001-09-01

ATP synthase--a marvellous rotary engine of the cell

Toru Hisabori
2001-04-01

The preferred stoichiometry of c subunits in the rotary motor sector of Escherichia coli ATP synthase is 10.
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Structural changes linked to proton translocation by subunit c of the ATP synthase
1999-03

Protein backbone angle restraints from searching a database for chemical shift and sequence homology

Gabriel Cornilescu, Ad Bax
1999-08-01

Practical methods for solid-state NMR distance measurements on large biomolecules: constant-time rotational resonance
1999-11-26

Molecular architecture of the rotary motor in ATP synthase
1999-07-01

Structure of the subunit c oligomer in the F1Fo ATP synthase: model derived from solution structure of the monomer and cross-linking in the native enzyme
1998-06-23

Solution structure of the transmembrane H+-transporting subunit c of the F1F0 ATP synthase
1998-06-01

Interacting helical faces of subunits a and c in the F1Fo ATP synthase of Escherichia coli defined by disulfide cross-linking
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The ATP synthase--a splendid molecular machine

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