Three-dimensional structure of a type VI turn in a linear peptide in water solution Evidence for stacking of aromatic rings as a major stabilizing factor
- 4 November 1994
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 243 (4) , 754-766
- https://doi.org/10.1016/0022-2836(94)90045-0
Abstract
No abstract availableKeywords
This publication has 25 references indexed in Scilit:
- Influence of proline residues on protein conformationPublished by Elsevier ,2004
- Hydrogen bonding in globular proteinsPublished by Elsevier ,2003
- Defining Solution Conformations of Small Linear PeptidesAnnual Review of Biophysics, 1991
- Three-dimensional solution structure of the reduced form of Escherichia coli thioredoxin determined by nuclear magnetic resonance spectroscopyBiochemistry, 1990
- Folding of immunogenic peptide fragments of proteins in water solutionJournal of Molecular Biology, 1988
- Correlation of connected transitions by two-dimensional NMR spectroscopyThe Journal of Chemical Physics, 1986
- The immunodominant site of a synthetic immunogen has a conformational preference in water for a type-II reverse turnNature, 1985
- Differences and sums of traces within, COSY spectra (DISCO) for the extraction of coupling constants: ‘Decoupling’ after the measurementMagnetic Resonance in Chemistry, 1985
- Structure determination of a tetrasaccharide: transient nuclear Overhauser effects in the rotating frameJournal of the American Chemical Society, 1984
- 1H-15N Spin-spin couplings in alumichromeBiopolymers, 1978