Conformational changes, dynamics and assignments in 1H NMR studies of proteins using ring current calculations Hen egg white lysozyme
- 19 October 1977
- journal article
- Published by Wiley in FEBS Letters
- Vol. 82 (1), 17-22
- https://doi.org/10.1016/0014-5793(77)80876-4
Abstract
No abstract availableThis publication has 18 references indexed in Scilit:
- Hydrogen‐deuterium exchange of the tryptophan residues in bovine α‐lactalbuminBiopolymers, 1976
- Nuclear magnetic resonance studies on the structure of lysozyme in solutionProceedings of the Royal Society of London. Series A. Mathematical and Physical Sciences, 1975
- Assignment of the 1 H n.m.r. spectra of proteinsProceedings of the Royal Society of London. Series A. Mathematical and Physical Sciences, 1975
- Proton magnetic resonance studies of the tyrosine residues of hen lysozyme-assignment and detection of conformational mobilityProceedings of the Royal Society of London. B. Biological Sciences, 1975
- Real-space refinement of the structure of hen egg-white lysozymeJournal of Molecular Biology, 1974
- Proton magnetic resonance of non-planar condensed benzenoid hydrocarbonsMolecular Physics, 1971
- An Investigation of the Conformation of Bovine α‐Lactalbumin by Proton Magnetic Resonance and Optical SpectroscopyEuropean Journal of Biochemistry, 1970
- Proton magnetic resonance spectra of proteins in random-coil configurationsJournal of the American Chemical Society, 1969
- Magnetic Resonance Studies of Macromolecules. I. Aromatic-Methyl Interactions and Helical Structure Effects in Lysozyme*Biochemistry, 1967
- Calculation of Nuclear Magnetic Resonance Spectra of Aromatic HydrocarbonsThe Journal of Chemical Physics, 1958