The Cold Denatured State Is Compact but Expands at Low Temperatures: Hydrodynamic Properties of the Cold Denatured State of the C-terminal Domain of L9-Reference-Cited by-同舟云学术

The Cold Denatured State Is Compact but Expands at Low Temperatures: Hydrodynamic Properties of the Cold Denatured State of the C-terminal Domain of L9

Published:2007-04 Issue:1 Volume:368 Page:256-262
ISSN:0022-2836
Container-title:Journal of Molecular Biology
language:en
Short-container-title:Journal of Molecular Biology

Author:

Li Ying,Shan Bing,Raleigh Daniel P.

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference39 articles.

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2. The concept of a random coil. Residual structure in peptides and denatured proteins;Smith;Fold. Des.,1996

3. NMR studies of unfolded states of an SH3 domain in aqueous solution and denaturing conditions;Zhang;Biochemistry,1997

4. Structural characterization of folded and unfolded states of an SH3 domain in equilibrium in aqueous buffer;Zhang;Biochemistry,1995

5. NOE data demonstrating a compact unfolded state for an SH3 domain under non-denaturing conditions;Mok;J. Mol. Biol.,1999

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