Chemical denaturation and elevated folding temperatures are required for wild-type activity and stability of recombinant Methanococcus jannaschii 20S proteasome-Reference-Cited by-同舟云学术

Chemical denaturation and elevated folding temperatures are required for wild-type activity and stability of recombinant Methanococcus jannaschii 20S proteasome

Published:2009-04-13 Issue:9 Volume:10 Page:1887-1896
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Frankenberg Rob J.,Hsu Tina S.,Yakota Hisao,Kim Rosalind,Clark Douglas S.

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Reference27 articles.

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5. Heterologous expression of 5′-methylthioadenosine phosphorylase from the archaeon Sulfolobus solfataricus : Characterization of the recombinant protein and involvement of disulfide bonds in thermophilicity and thermostability;Cacciapuoti;Protein Expres. Purif.,1999

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3. Archaean Proteasome;Handbook of Proteolytic Enzymes;2013

4. Nature Versus Nurture: Developing Enzymes That Function Under Extreme Conditions;Annual Review of Chemical and Biomolecular Engineering;2012-07-15

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