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Site-directed <sup>13</sup>C solid-state NMR studies on membrane proteins: strategy and goals toward revealing conformation and dynamics as illustrated for bacteriorhodopsin labeled with [1-<sup>13</sup>C]amino acid residues.
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- Magnetic Resonance in Chemistry, 2004, v. 42, n. 2, p. 218, doi. 10.1002/mrc.1325
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Cytoplasmic surface structures of bacteriorhodopsin modified by site-directed mutations and cation binding as revealed by [sup 13] C NMR.
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- European Biophysics Journal, 2003, v. 32, n. 1, p. 1, doi. 10.1007/s00249-002-0260-0
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<sup>13</sup>C-nmr chemical shift and conformation of L-alanine residues incorporated into poly(β-benzyl L-aspartate) in the solid state.
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- Biopolymers, 1987, v. 26, n. 12, p. 1983, doi. 10.1002/bip.360261202
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Phosphatidylserine induces functional and structural alterations of the membrane-associated pleckstrin homology domain of phospholipase C-δ1.
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- FEBS Journal, 2007, v. 274, n. 1, p. 177, doi. 10.1111/j.1742-4658.2006.05574.x
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Membrane-induced alteration of the secondary structure in the SWAP-70 pleckstrin homology domain.
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- Journal of Biochemistry, 2012, v. 151, n. 4, p. 391, doi. 10.1093/jb/mvr146
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Surface Dynamics of Bacteriorhodopsin as Revealed by 13C NMR Studies on [13C]Ala-Labeled Proteins: Detection of Millisecond or Microsecond Motions in Interhelical Loops and C-Terminal α-Helix1.
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- Journal of Biochemistry, 2001, v. 129, n. 3, p. 373, doi. 10.1093/oxfordjournals.jbchem.a002867
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- Article
Irreversible Conformational Change of Bacterio-opsin Induced by Binding of Retinal during Its Reconstitution to Bacteriorhodopsin, as Studied by 13NMR1.
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- Journal of Biochemistry, 2000, v. 127, n. 5, p. 861, doi. 10.1093/oxfordjournals.jbchem.a022680
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- Article
Dynamics and orientation of transmembrane peptide from bacteriorhodopsin incorporated into lipid bilayer as revealed by solid state <sup>31</sup>P and <sup>13</sup>C NMR spectroscopy.
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- Biopolymers, 2002, v. 63, n. 2, p. 122, doi. 10.1002/bip.10021
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- Article
A <sup>13</sup>C NMR study on [3-<sup>13</sup>C]-, [1-<sup>13</sup>C]Ala-, or [1-<sup>13</sup>C]Val-labeled transmembrane peptides of bacteriorhodopsin in lipid bilayers: Insertion, rigid-body motions, and local conformational fluctuations at ambient temperature
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- Biopolymers, 2001, v. 58, n. 1, p. 78, doi. 10.1002/1097-0282(200101)58:1<78::AID-BIP80>3.0.CO;2-C
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- Article
Significance of low-frequency local fluctuation motions in the transmembrane B and C a-helices of bacteriorhodopsin, to facilitate efficient proton uptake from the cytoplasmic surface, as revealed by site-directed solid-state<sup>13</sup>C NMR.
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- European Biophysics Journal, 2004, v. 33, n. 7, p. 580, doi. 10.1007/s00249-004-0406-3
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Dynamic structure of pharaonis phoborhodopsin (sensory rhodopsin II) and complex with a cognate truncated transducer as revealed by site-directed <sup>13</sup>C solid-state NMR
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- FEBS Letters, 2003, v. 536, n. 1-3, p. 237, doi. 10.1016/S0014-5793(03)00065-6
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Conformational transitions and fibrillation mechanism of human calcitonin as studied by high-resolution solid-state 13C NMR.
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- Protein Science: A Publication of the Protein Society, 2000, v. 9, n. 5, p. 867
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Direct Evidence of Interaction of a Green Tea Polyphenol, Epigallocatechin Gallate, with Lipid Bilayers by Solid-state Nuclear Magnetic Resonance.
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- Bioscience, Biotechnology & Biochemistry, 2004, v. 68, n. 8, p. 1743, doi. 10.1271/bbb.68.1743
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Stability of the C-Terminal α-Helical Domain of Bacteriorhodopsin That Protrudes from the Membrane Surface, as Studied by High-Resolution Solid-State 13C NMR1.
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- Journal of Biochemistry, 1998, v. 123, n. 1, p. 78, doi. 10.1093/oxfordjournals.jbchem.a021919
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Participation of the BC Loop in the Correct Folding of Bacteriorhodopsin as Revealed by Solid-state NMR.
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- Photochemistry & Photobiology, 2009, v. 85, n. 2, p. 624, doi. 10.1111/j.1751-1097.2009.00536.x
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Dynamics Change of Phoborhodopsin and Transducer by Activation: Study Using D75N Mutant of the Receptor by Site-directed Solid-state <sup>13</sup>C NMR.
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- Photochemistry & Photobiology, 2008, v. 84, n. 4, p. 921, doi. 10.1111/j.1751-1097.2008.00326.x
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Participation of the Surface Structure of Pharaonis Phoborhodopsin, ppR and its A149S and A149V mutants, Consisting of the C-terminal α-helix and E–F Loop, in the Complex-formation with the Cognate Transducer pHtrII, as Revealed by Site-directed <sup>13</sup>C Solid-state NMR
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- Photochemistry & Photobiology, 2007, v. 83, n. 2, p. 339, doi. 10.1562/2006-06-20-RA-940
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Pressure-induced Isomerization of Retinal on Bacteriorhodopsin as Disclosed by Fast Magic Angle Spinning NMR.
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- Photochemistry & Photobiology, 2007, v. 83, n. 2, p. 346, doi. 10.1562/2006-06-20-RC-941
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Surface and Dynamic Structures of Bacteriorhodopsin in a 2D Crystal, a Distorted or Disrupted Lattice, as Revealed by Site-directed Solid-state <sup>13</sup>C NMR.
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- Photochemistry & Photobiology, 2007, v. 83, n. 2, p. 253, doi. 10.1562/2006.06-12-IR-917
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