Unfolding of apomyoglobin from Aplysia limacina: the effect of salt and ph on the cooperativity of folding
- 9 January 1998
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 275 (1), 133-148
- https://doi.org/10.1006/jmbi.1997.1409
Abstract
No abstract availableKeywords
This publication has 56 references indexed in Scilit:
- How Hofmeister ion interactions affect protein stabilityBiophysical Journal, 1996
- Impact of Local and Non-local Interactions on Thermodynamics and Kinetics of Protein FoldingJournal of Molecular Biology, 1995
- Molecular Mechanisms of Acid Denaturation: The Role of Histidine Residues in the Partial Unfolding of ApomyoglobinJournal of Molecular Biology, 1994
- Three-state analysis of sperm whale apomyoglobin foldingBiochemistry, 1993
- Pulsed H/D-exchange studies of folding intermediatesCurrent Opinion in Structural Biology, 1993
- Solvent denaturation and stabilization of globular proteinsBiochemistry, 1991
- X-ray crystal structure of the fluoride derivative of Aplysia limacina ferric myoglobin at 2·0 Å resolutionJournal of Molecular Biology, 1990
- Aplysia limacina myoglobinJournal of Molecular Biology, 1989
- Diffusion‐collision model for the folding kinetics of myoglobinProteins-Structure Function and Bioinformatics, 1988
- Fluorescence studies of Aplysia and sperm whale apomyoglobinsBiochemistry, 1970