Dynamic aspect of bacteriorhodopsin as a typical membrane protein as revealed by site-directed solid-state 13C NMR
- 31 January 2004
- journal article
- research article
- Published by Elsevier in Solid State Nuclear Magnetic Resonance
- Vol. 25 (1-3) , 5-14
- https://doi.org/10.1016/j.ssnmr.2003.06.001
Abstract
No abstract availableKeywords
This publication has 29 references indexed in Scilit:
- Conformation and backbone dynamics of bacteriorhodopsin revealed by 13C-NMRBiochimica et Biophysica Acta (BBA) - Bioenergetics, 2000
- SOLID-STATE NUCLEAR MAGNETIC RESONANCE INVESTIGATION OF PROTEIN AND POLYPEPTIDE STRUCTUREAnnual Review of Biophysics, 1999
- Lipid patches in membrane protein oligomers: Crystal structure of the bacteriorhodopsin-lipid complexProceedings of the National Academy of Sciences, 1998
- Proton Transfer Pathways in Bacteriorhodopsin at 2.3 Angstrom ResolutionScience, 1998
- Empirical Versus N On Empirical Evaluation Of Secondary Structure Of Fibrous And Membrane Proteins By Solid-State Nmr: A Practical ApproachPublished by Elsevier ,1998
- X-ray Structure of Bacteriorhodopsin at 2.5 Angstroms from Microcrystals Grown in Lipidic Cubic PhasesScience, 1997
- Electron-crystallographic Refinement of the Structure of BacteriorhodopsinJournal of Molecular Biology, 1996
- High-Resolution Solid-State NMR Studies of Synthetic and Biological MacromoleculesPublished by Elsevier ,1989
- Protein structure by solid-state NMR spectroscopyQuarterly Reviews of Biophysics, 1987
- Conformation‐dependent 13C chemical shifts: A new means of conformational characterization as obtained by high‐resolution solid‐state 13C NMRMagnetic Resonance in Chemistry, 1986