A proposed mechanism for the thermal denaturation of a recombinant Bacillus halmapalus α-amylase—the effect of calcium ions
- 1 November 2003
- journal article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
- Vol. 1652 (1) , 52-63
- https://doi.org/10.1016/j.bbapap.2003.08.002
Abstract
No abstract availableKeywords
This publication has 40 references indexed in Scilit:
- Effect of calcium ions on the irreversible denaturation of a recombinant Bacillus halmapalus alpha-amylase: a calorimetric investigationBiochemical Journal, 2003
- Chemical modification of bacterial α-amylases: changes in tertiary structures and the effect of additional calciumBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 2001
- Protein engineering of bacterial α-amylasesBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 2000
- Probing structural determinants specifying high thermostability in Bacillus licheniformis α-amylase 1 1Edited by A. R. FershtJournal of Molecular Biology, 2000
- Development of Industrially Important .ALPHA.-Amylases.Journal of Applied Glycoscience, 1999
- Crystal Structure of Calcium-depletedBacillus licheniformisα-amylase at 2.2 Å ResolutionJournal of Molecular Biology, 1995
- Thermal transitions in the purple membrane from Halobacterium halobiumFEBS Letters, 1993
- Differential scanning calorimetric study of carboxypeptidase B, procarboxypeptidase B and its globular activation domainEuropean Journal of Biochemistry, 1991
- Differential scanning calorimetric study of the thermal unfolding of Taka-amylase A from Aspergillus oryzaeBiochemistry, 1987
- Calorimetric measurements of the effect of 330‐MHz radiofrequency radiation on human erythrocyte ghostsBioelectromagnetics, 1984