Submillisecond Unfolding Kinetics of Apomyoglobin and its pH 4 Intermediate
Open Access
- 1 September 1999
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 292 (3) , 731-740
- https://doi.org/10.1006/jmbi.1999.3074
Abstract
No abstract availableKeywords
This publication has 32 references indexed in Scilit:
- CytochromecFolding and Unfolding: A Biphasic MechanismAccounts of Chemical Research, 1998
- Two forms of the pH 4 folding intermediate of apomyoglobinJournal of Molecular Biology, 1998
- Folding intermediates of wild-type and mutants of barnase. I. use of φ-value analysis and m-values to probe the cooperative nature of the folding pre-equilibriumJournal of Molecular Biology, 1998
- Three-state model for lysozyme folding: triangular folding mechanism with an energetically trapped intermediateJournal of Molecular Biology, 1997
- Direct Measurement of Nucleation and Growth Rates in Lysozyme FoldingBiochemistry, 1997
- Kinetics of Folding of the IgG Binding Domain of Peptostreptoccocal Protein LBiochemistry, 1997
- Cold Denaturation of the Molten Globule States of Apomyoglobin and a Profile for Protein FoldingBiochemistry, 1994
- A Kinetic Method to Evaluate the Two-State Character of Solvent-Induced Protein DenaturationBiochemistry, 1994
- Thermodynamic study of the apomyoglobin structureJournal of Molecular Biology, 1988
- Studies on the structure of hemoglobin I. Physicochemical properties of human globinBiochimica et Biophysica Acta, 1958