Identification and description of β-structure in horse muscle acylphosphatase by nuclear magnetic resonance spectroscopy
- 1 May 1989
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 207 (2), 405-415
- https://doi.org/10.1016/0022-2836(89)90263-5
Abstract
No abstract availableThis publication has 16 references indexed in Scilit:
- Identification and description of α-helical regions in horse muscle acylphosphatase by 1H nuclear magnetic resonance spectroscopyJournal of Molecular Biology, 1989
- Folding of immunogenic peptide fragments of proteins in water solutionJournal of Molecular Biology, 1988
- Secondary structure of acylphosphatase from rabbit skeletal muscle: A nuclear magnetic resonance studyJournal of Molecular Biology, 1988
- Protein structures in solution by nuclear magnetic resonance and distance geometryJournal of Molecular Biology, 1987
- Structural and sequence patterns in the loops of βαβ unitsProtein Engineering, Design and Selection, 1987
- Calculation of protein conformations by proton-proton distance constraintsJournal of Molecular Biology, 1985
- Calibration of the angular dependence of the amide proton-Cα proton coupling constants, 3JHNα, in a globular proteinJournal of Molecular Biology, 1984
- Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonanceJournal of Molecular Biology, 1983
- Structural information from NMR secondary chemical shifts of peptide α C-H protons in proteinsBioscience Reports, 1983
- Amide proton exchange and surface conformation of the basic pancreatic trypsin inhibitor in solutionJournal of Molecular Biology, 1982