Protein thermostability above 100 C: A key role for ionic interactions-Reference-Cited by-同舟云学术

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Protein thermostability above 100 C: A key role for ionic interactions

Published:1998-10-13 Issue:21 Volume:95 Page:12300-12305
ISSN:0027-8424
Container-title:Proceedings of the National Academy of Sciences
language:en
Short-container-title:Proceedings of the National Academy of Sciences

Author:

Vetriani C.,Maeder D. L.,Tolliday N.,Yip K. S.- P.,Stillman T. J.,Britton K. L.,Rice D. W.,Klump H. H.,Robb F. T.

Publisher

Proceedings of the National Academy of Sciences

Subject

Multidisciplinary

Reference38 articles.

1. ENZYMES AND PROTEINS FROM ORGANISMS THAT GROW NEAR AND ABOVE 100°C

2. Structure of a Hyperthermophilic Tungstopterin Enzyme, Aldehyde Ferredoxin Oxidoreductase

3. Hydrophobic core repacking and aromatic-aromatic interaction in the thermostable mutant of T4 lysozyme ser 117 → phe

4. Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme

5. Insights into Thermal Stability from a Comparison of the Glutamate Dehydrogenases from Pyrococcus furiosus and Thermococcus litoralis

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