Molecular structure of a barley α-amylase-inhibitor complex: implications for starch binding and catalysis
- 1 April 1998
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 278 (1) , 205-217
- https://doi.org/10.1006/jmbi.1998.1683
Abstract
No abstract availableKeywords
This publication has 62 references indexed in Scilit:
- Mechanism-based Inhibition of Yeast α-Glucosidase and Human Pancreatic α-Amylase by a New Class of InhibitorsJournal of Biological Chemistry, 1995
- Structures and mechanisms of glycosyl hydrolasesStructure, 1995
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- Barley malt-α-amylase. Purication, action pattern, and subsite mapping of isozyme 1 and two members of the isozyme 2 subfamily using p-nitrophenylated maltooligosaccharide substratesBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1992
- Free R value: a novel statistical quantity for assessing the accuracy of crystal structuresNature, 1992
- Solution of the structure of Aspergillus niger acid α-amylase by combined molecular replacement and multiple isomorphous replacement methodsActa crystallographica Section B, Structural science, crystal engineering and materials, 1991
- Calcium binding in .alpha.-amylases: an x-ray diffraction study at 2.1-.ANG. resolution of two enzymes from AspergillusBiochemistry, 1990
- A fast algorithm for rendering space-filling molecule picturesJournal of Molecular Graphics, 1988
- Crystallographic R Factor Refinement by Molecular DynamicsScience, 1987
- The solution conformation of acarboseCarbohydrate Research, 1984