Calcium Binding and Thermostability of Carbohydrate Binding Module CBM4-2 of Xyn10A from Rhodothermus marinus-Reference-Cited by-同舟云学术

Calcium Binding and Thermostability of Carbohydrate Binding Module CBM4-2 of Xyn10A from Rhodothermus marinus

Published:2002-04-16 Issue:18 Volume:41 Page:5720-5729
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Abou-Hachem Maher¹,Karlsson Eva Nordberg¹,Simpson Peter J.¹,Linse Sara¹,Sellers Peter¹,Williamson Michael P.¹,Jamieson Stuart J.¹,Gilbert Harry J.¹,Bolam David N.¹,Holst Olle¹

Affiliation:

1. Department of Biotechnology, Center for Chemistry and Chemical Engineering, Lund University, P.O. Box 124, SE-221 00 Lund, Sweden, Krebs Institute, Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield S10 2TN, U.K., Department of Biophysical Chemistry, Center for Chemistry and Chemical Engineering, Lund University, P.O. Box 124, SE-221 00 Lund, Sweden, and Department of Biological and Nutritional Sciences, University of Newcastle upon Tyne, Newcastle upon Tyne NE1 7RU, U.K.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi012094a

Reference47 articles.

1. Three dimensional structure of porcine pancreatic alpha-amylase at 2.9 A resolution. Role of calcium in structure and activity.

2. Kinetic study of the irreversible thermal denaturation of Bacillus licheniformis α-amylase

3. Probing structural determinants specifying high thermostability in Bacillus licheniformis α-amylase 1 1Edited by A. R. Fersht

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