Comparison of the chemical and thermal denaturation of proteins by a two-state transition model-Reference-Cited by-同舟云学术

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Comparison of the chemical and thermal denaturation of proteins by a two-state transition model

Published:2008-03 Issue:1 Volume:374 Page:221-230
ISSN:0003-2697
Container-title:Analytical Biochemistry
language:en
Short-container-title:Analytical Biochemistry

Author:

Ramprakash J.,Doseeva V.,Galkin A.,Krajewski W.,Muthukumar L.,Pullalarevu S.,Demirkan E.,Herzberg O.,Moult J.,Schwarz F.P.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference25 articles.

1. Determination and analysis of urea and guanidine hydrochloride denaturation curves;Pace;Methods Enzymol.,1986

2. A thermodynamic approach to the problem of stabilization of globular protein structure: A calorimetric study;Privalov;J. Mol. Biol.,1974

3. Thermodynamics of denaturation of staphylococcal nuclease mutants: An intermediate state in protein folding;Carra;FASEB J.,1996

4. Chemical denaturation: Potential impact of undetected intermediates in the free energy of unfolding and m-values obtained from a two-state assumption;Soulages;Biophys. J.,1998

5. The role of chaperones in Parkinson’s disease and prion diseases;Winklhofer,2006

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