Solid-state NMR structural studies of peptides and proteins in membranes
Open Access
- 1 January 1994
- journal article
- Published by Elsevier in Current Opinion in Structural Biology
- Vol. 4 (4) , 574-581
- https://doi.org/10.1016/s0959-440x(94)90220-8
Abstract
No abstract availableThis publication has 44 references indexed in Scilit:
- Magic angle spinning NMR methods for internuclear distance measurementsCurrent Opinion in Structural Biology, 1993
- 2H NMR lineshapes of immobilized uniaxially oriented membrane proteinsSolid State Nuclear Magnetic Resonance, 1993
- Determination of the molecular conformation of melanostatin using carbon-13, nitrogen-15 REDOR NMR spectroscopyJournal of the American Chemical Society, 1993
- Rotational resonance NMR study of the active site structure in bacteriorhodopsin: conformation of the Schiff base linkageBiochemistry, 1992
- Determination of an 8-.ANG. interatomic distance in a helical peptide by solid-state NMR spectroscopyJournal of the American Chemical Society, 1992
- Orientations of amphipathic helical peptides in membrane bilayers determined by solid-state NMR spectroscopyJournal of Biomolecular NMR, 1991
- Experimental determination of torsion angles in the polypeptide backbone of the gramicidin a channel by solid state nuclear magnetic resonanceJournal of Molecular Biology, 1991
- Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopyJournal of Molecular Biology, 1990
- Protein structure by solid-state NMR spectroscopyQuarterly Reviews of Biophysics, 1987
- Two-dimensional 13C NMR of highly oriented polyethyleneThe Journal of Chemical Physics, 1977