Glyceraldehyde-3-Phosphate Dehydrogenases from Archaea: Objects for Studying Protein Thermoadaptation
Author:
Affiliation:
1. FB 9 Mikrobiologie, Universität GHS Essen, Universitätsstr 5, D-45117 Essen
2. Lehrstuhl für Genetik, der Universität Regensburg, D-8400, Regensburg
3. Max-Planck-Institut fur Biochemie, Am Klopferspitz, D-82152, Martinsried
Publisher
Informa UK Limited
Subject
General Agricultural and Biological Sciences,Biochemistry,Biotechnology,Catalysis
Link
https://www.tandfonline.com/doi/pdf/10.3109/10242429409034385
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1. Protein thermal stabilization by charged compatible solutes: Computational studies in rubredoxin from Desulfovibrio gigas;Proteins: Structure, Function, and Bioinformatics;2008-02-04
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3. Functional characterization of the phosphorylating D-glyceraldehyde 3-phosphate dehydrogenase from the archaeon Methanothermus fervidus by comparative molecular modelling and site-directed mutagenesis;European Journal of Biochemistry;1999-10
4. Sequence and structural comparison of thermophilic phosphoglycerate kinases with a mesophilic equivalent;Comparative Biochemistry and Physiology Part A: Physiology;1997-11
5. Phosphoribosyl anthranilate isomerase fromThermotoga maritimais an extremely stable and active homodimer;Protein Science;1996-10
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