1H NMR studies on an Asn-linked glycopeptide. GlcNAc-1 C2-N2 bond is rigid in H2O.
Open Access
- 1 February 1994
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 269 (5), 3331-3338
- https://doi.org/10.1016/s0021-9258(17)41867-9
Abstract
No abstract availableKeywords
This publication has 46 references indexed in Scilit:
- Effects of glycosylation on protein conformation and amide proton exchange rates in RNase BFEBS Letters, 1992
- Hydrogen exchange in thermally denatured ribonucleaseBiochemistry, 1991
- Solution structure of a synthetic N-glycosylated cyclic hexapeptide determined by NMR spectroscopy and MD calculationsJournal of the American Chemical Society, 1991
- One- and two-dimensional NMR studies of the N-terminal portion of glycophorin A at 11.7 TeslaProtein Journal, 1990
- Hydroxyl and amido groups as long-range sensors in conformational analysis by nuclear Overhauser enhancement: a source of experimental evidence for conformational flexibility of oligosaccharidesJournal of the American Chemical Society, 1989
- Folding of immunogenic peptide fragments of proteins in water solutionJournal of Molecular Biology, 1988
- 13C-NMR spectral studies of the n—terminal portion of glycophorinsProgress in Nuclear Magnetic Resonance Spectroscopy, 1986
- Conformational energy calculations on glycosylated turns in glycoproteinsBiopolymers, 1982
- Fourier transform multiple quantum nuclear magnetic resonanceFaraday Symposia of the Chemical Society, 1978
- Conformational energy calculations of enzyme‐substrate complexes of lysozyme. I. Energy minimization of monosaccharide and oligosaccharide inhibitors and substrates of lysozymeBiopolymers, 1976