How does trimethylamine N-oxide counteract the denaturing activity of urea?
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Title
How does trimethylamine N-oxide counteract the denaturing activity of urea?
Authors
Keywords
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Journal
PHYSICAL CHEMISTRY CHEMICAL PHYSICS
Volume 13, Issue 39, Pages 17689
Publisher
Royal Society of Chemistry (RSC)
Online
2011-09-06
DOI
10.1039/c1cp22176k
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- (2011) Deepak R. Canchi et al. BIOPHYSICAL JOURNAL
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- On the stability of chymotrypsin inhibitor 2 in a 10 M urea solution. The role of interaction energies for urea-induced protein denaturation
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- Urea, but not guanidinium, destabilizes proteins by forming hydrogen bonds to the peptide group
- (2009) Woon Ki Lim et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Structure and Energetics of the Hydrogen-Bonded Backbone in Protein Folding
- (2008) D. Wayne Bolen et al. Annual Review of Biochemistry
- Salting out of methane by sodium chloride: A scaled particle theory study
- (2008) Giuseppe Graziano JOURNAL OF CHEMICAL PHYSICS
- Urea denaturation by stronger dispersion interactions with proteins than water implies a 2-stage unfolding
- (2008) L. Hua et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Effect of osmolyte or GdnHCl on volumetric properties of aqueous solutions containing cyclic dipeptides
- (2007) Pannur Venkatesu et al. BIOCHEMICAL ENGINEERING JOURNAL
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