Trifluoroethanol stabilizes the pH 4 folding intermediate of sperm whale apomyoglobin
Authors:
- Yongzhang LuoaYongzhang Luoa
- Robert L BaldwinRBRobert L Baldwin
Open Access
- 1 May 1998
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 279 (1) , 49-57
Abstract
No abstract availableKeywords
This publication has 42 references indexed in Scilit:
- Two forms of the pH 4 folding intermediate of apomyoglobinJournal of Molecular Biology, 1998
- Formation of a Molten-Globule-like State of Myoglobin in Aqueous HexafluoroisopropanolBiochemical and Biophysical Research Communications, 1997
- Helix propagation and N‐cap propensities of the amino acids measured in alanine‐based peptides in 40 volume percent trifluoroethanolProtein Science, 1996
- Intrinsic Stability of Individual α Helices Modulates Structure and Stability of the Apomyoglobulin Molten Globule FormJournal of Molecular Biology, 1995
- Trifluoroethanol-induced Stabilization of the α-Helical Structure of β-Lactoglobulin: Implication for Non-hierarchical Protein FoldingJournal of Molecular Biology, 1995
- Contribution of the hydrophobic effect to globular protein stabilityJournal of Molecular Biology, 1992
- Folding of immunogenic peptide fragments of proteins in water solutionJournal of Molecular Biology, 1988
- Thermodynamics of protein denaturation. III. Denaturation of ribonuclease in water and in aqueous urea and aqueous ethanol mixturesJournal of the American Chemical Society, 1967
- The Effect of Protein Denaturants on the Stability of the α Helix1Journal of the American Chemical Society, 1966
- Contribution of Hydrophobic Interactions to the Stability of the Globular Conformation of ProteinsJournal of the American Chemical Society, 1962