pH Dependence of Stability of Staphylococcal Nuclease: Evidence of Substantial Electrostatic Interactions in the Denatured State
- 21 October 2000
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 39 (46), 14292-14304
- https://doi.org/10.1021/bi001015c
Abstract
No abstract availableKeywords
This publication has 32 references indexed in Scilit:
- Global Analysis of the Acid-Induced and Urea-Induced Unfolding of Staphylococcal Nuclease and Two of Its VariantsBiochemistry, 1997
- Equilibrium folding pathway of staphylococcal nuclease: identification of the most stable chain-chain interactions by NMR and CD spectroscopyBiochemistry, 1995
- Perturbed pKA-values in the Denatured States of ProteinsJournal of Molecular Biology, 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
- Hydrogen Bonds and the pH dependence of Ovomucoid Third Domain StabilityBiochemistry, 1995
- Thermodynamic study of the acid denaturation of barnase and its dependence on ionic strength: Evidence for residual electrostatic interactions in the acid/thermally denatured stateBiochemistry, 1994
- Prediction of Ph-dependent Properties of ProteinsJournal of Molecular Biology, 1994
- Molecular Mechanisms of Acid Denaturation: The Role of Histidine Residues in the Partial Unfolding of ApomyoglobinJournal of Molecular Biology, 1994
- Unfolding free energy changes determined by the linear extrapolation method. 2. Incorporation of .DELTA.G.degree.N-U values in a thermodynamic cycleBiochemistry, 1988
- Folding of staphylococcal nuclease: Kinetic studies of two processes in acid renaturationJournal of Molecular Biology, 1971