A Solid-State NMR Index of Helical Membrane Protein Structure and Topology
- 1 May 2000
- journal article
- editorial
- Published by Elsevier in Journal of Magnetic Resonance
- Vol. 144 (1), 150-155
- https://doi.org/10.1006/jmre.2000.2035
Abstract
No abstract availableKeywords
This publication has 30 references indexed in Scilit:
- Model-Independent Analysis of 15N Chemical Shift Anisotropy from NMR Relaxation Data. Ubiquitin as a Test ExampleJournal of the American Chemical Society, 1998
- Dipolar recoupling in MAS spectra of biological solidsNature Structural & Molecular Biology, 1998
- Solid‐state NMR studies of the membrane‐bound closed state of the colicin E1 channel domain in lipid bilayersProtein Science, 1998
- Helix packing in membrane proteinsJournal of Molecular Biology, 1997
- Magic angle spinning NMR spectroscopy of membrane proteinsQuarterly Reviews of Biophysics, 1996
- High-resolution NMR of biological solidsCurrent Opinion in Structural Biology, 1996
- Simultaneous Characterization of the Amide 1H Chemical Shift, 1H-15N Dipolar, and 15N Chemical Shift Interaction Tensors in a Peptide Bond by Three-Dimensional Solid-State NMR SpectroscopyJournal of the American Chemical Society, 1995
- Solid-state NMR structural studies of peptides and proteins in membranesCurrent Opinion in Structural Biology, 1994
- Orientational constraints as three‐dimensional structural constraints from chemical shift anisotropy: The polypeptide backbone of gramicidin A in a lipid bilayerProtein Science, 1993
- The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopyBiochemistry, 1992