Thermodynamics and Kinetics of Non-native Interactions in Protein Folding: A Single Point Mutant Significantly Stabilizes the N-terminal Domain of L9 by Modulating Non-native Interactions in the Denatured State-Reference-Cited by-同舟云学术

Thermodynamics and Kinetics of Non-native Interactions in Protein Folding: A Single Point Mutant Significantly Stabilizes the N-terminal Domain of L9 by Modulating Non-native Interactions in the Denatured State

Published:2004-05 Issue:4 Volume:338 Page:827-837
ISSN:0022-2836
Container-title:Journal of Molecular Biology
language:en
Short-container-title:Journal of Molecular Biology

Author:

Cho Jae-Hyun,Sato Satoshi,Raleigh Daniel P.

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference38 articles.

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3. The denatured state (the other half of the folding equation) and its role in protein stability;Shortle;FASEB J.,1996

4. Toward a taxonomy of the denatured state: small angle scattering studies of unfolded proteins;Millett;Advan. Protein Chem.,2002

5. A new perspective on unfolded proteins;Baldwin;Advan. Protein Chem.,2002

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