Analysis of the pH-dependent Folding and Stability of Histidine Point Mutants Allows Characterization of the Denatured State and Transition State for Protein Folding
- 7 January 2005
- journal article
- Published by Elsevier BV in Journal of Molecular Biology
- Vol. 345 (1), 163-173
- https://doi.org/10.1016/j.jmb.2004.10.023
Abstract
No abstract availableKeywords
This publication has 38 references indexed in Scilit:
- Distribution of molecular size within an unfolded state ensemble using small-angle X-ray scattering and pulse field gradient NMR techniquesJournal of Molecular Biology, 2002
- A model of the changes in denatured state structure underlying m value effects in staphylococcal nuclease.Nature Structural & Molecular Biology, 1999
- pKa Values and the pH Dependent Stability of the N-Terminal Domain of L9 as Probes of Electrostatic Interactions in the Denatured State. Differentiation between Local and Nonlocal InteractionsBiochemistry, 1999
- Formation of Electrostatic Interactions on the Protein-Folding PathwayBiochemistry, 1996
- The denatured state (the other half of the folding equation) and its role in protein stabilityThe FASEB Journal, 1996
- Perturbed pKA-values in the Denatured States of ProteinsJournal of Molecular Biology, 1995
- Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfoldingProtein Science, 1995
- pKA Values of Carboxyl Groups in the Native and Denatured States of Barnase: The pKA Values of the Denatured State Are on Average 0.4 Units Lower Than Those of Model CompoundsBiochemistry, 1995
- Urea denaturation of barnase: pH dependence and characterization of the unfolded stateBiochemistry, 1992
- DENATURED STATES OF PROTEINSAnnual Review of Biochemistry, 1991