Thermodynamics of Protein Interactions with Urea and Guanidinium Hydrochloride
- 25 May 1999
- journal article
- other
- Published by American Chemical Society (ACS) in The Journal of Physical Chemistry B
- Vol. 103 (23), 4781-4785
- https://doi.org/10.1021/jp990413q
Abstract
No abstract availableKeywords
This publication has 23 references indexed in Scilit:
- Linkage of protonation and anion binding to the folding of Sac7dJournal of Molecular Biology, 1998
- Guanidine Hydrochloride Unfolding of Peptide Helices: Separation of Denaturant and Salt EffectsBiochemistry, 1996
- Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfoldingProtein Science, 1995
- A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration rangeBiochemistry, 1992
- Solvent denaturation and stabilization of globular proteinsBiochemistry, 1991
- A simple model for salvation in mixed solventsBiophysical Chemistry, 1990
- Unfolding free energy changes determined by the linear extrapolation method. 2. Incorporation of .DELTA.G.degree.N-U values in a thermodynamic cycleBiochemistry, 1988
- [14]Determination and analysis of urea and guanidine hydrochloride denaturation curvesMethods in Enzymology, 1986
- The Stability of Globular ProteinCRC Critical Reviews in Biochemistry, 1975
- Urea and Guanidine Hydrochloride Denaturation of Ribonuclease, Lysozyme, α-Chymotrypsin, and b-LactoglobulinJournal of Biological Chemistry, 1974