Acceleration of the folding of hen lysozyme by trifluoroethanol
- 1 January 1997
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 265 (2) , 112-117
- https://doi.org/10.1006/jmbi.1996.0715
Abstract
No abstract availableKeywords
Funding Information
- Medical Research Council
- Royal Society
- Howard Hughes Medical Institute
- Engineering and Physical Sciences Research Council
- Biotechnology and Biological Sciences Research Council
This publication has 39 references indexed in Scilit:
- Main-chain Dynamics of a Partially Folded Protein:15N NMR Relaxation Measurements of Hen Egg White Lysozyme Denatured in TrifluoroethanolJournal of Molecular Biology, 1996
- Mechanism of Stabilization of Helical Conformations of Polypeptides by Water Containing TrifluoroethanolJournal of the American Chemical Society, 1996
- Solvent isotope effects on the refolding kinetics of hen egg‐white lysozymeProtein Science, 1996
- Characterization of Conformational Preferences in a Partly Folded Protein by Heteronuclear NMR Spectroscopy: Assignment and Secondary Structure Analysis of Hen Egg-White Lysozyme in TrifluoroethanolBiochemistry, 1995
- Nonlocal Interactions Stabilize Long Range Loops in the Initial Folding Intermediates of Reduced Bovine Pancreatic Trypsin InhibitorBiochemistry, 1995
- Understanding how proteins fold: the lysozyme story so farTrends in Biochemical Sciences, 1994
- A partially folded state of hen egg white lysozyme in trifluoroethanol: structural characterization and implications for protein foldingBiochemistry, 1993
- Kinetic resolution of peptide bond and side chain far-UV circular dichroism during the folding of hen egg white lysozymeBiochemistry, 1992
- Folding of peptide fragments comprising the complete sequence of proteinsJournal of Molecular Biology, 1992
- Thermodynamics of the denaturation of lysozyme by guanidine hydrochloride. II. Dependence on denaturant concentration at 25°Biochemistry, 1969