Crystal structure determination, refinement and the molecular model of the α-amylase inhibitor Hoe-467A
- 1 May 1986
- journal article
- Published by Elsevier BV in Journal of Molecular Biology
- Vol. 189 (2), 383-386
- https://doi.org/10.1016/0022-2836(86)90520-6
Abstract
No abstract availableKeywords
This publication has 16 references indexed in Scilit:
- Studies by 1H nuclear magnetic resonance and distance geometry of the solution conformation of the α-amylase inhibitor TendamistatJournal of Molecular Biology, 1986
- Secondary structure of the α-amylase polypeptide inhibitor Tendamistat from Streptomyces tendae determined in solution by 1H nuclear magnetic resonanceJournal of Molecular Biology, 1985
- Studies on an animal .ALPHA.-amylase inhibitor (Haim) from Streptomyces griseosporeus YM-25. Part III. Inhibitory effects of the proteinaceous .ALPHA.-amylase inhibitor Haim on animal .ALPHA.-amylase.Agricultural and Biological Chemistry, 1985
- Crystallographic structure of pig pancreas α amylase (2.9 Å resolution)Acta Crystallographica Section A Foundations of Crystallography, 1984
- Die Primärstruktur des α-Amylaseinhibitors Hoe 467A ausStreptomyces tendae4158. Eine neue Klasse von InhibitorenHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1983
- Computer-Generated Schematic Diagrams of Protein StructuresScience, 1982
- A graphics model building and refinement system for macromoleculesJournal of Applied Crystallography, 1978
- Crystallographic structure studies of an IgG molecule and an Fc fragmentNature, 1976
- Energy refinement of hen egg-white lysozymeJournal of Molecular Biology, 1974
- A method of absorption correction by X-ray intensity measurementsActa Crystallographica Section A, 1968