Clustering of Fluorine-Substituted Alcohols as a Factor Responsible for Their Marked Effects on Proteins and Peptides
Authors:
- 5 August 1999
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 121 (37) , 8427-8433
Abstract
No abstract availableKeywords
This publication has 31 references indexed in Scilit:
- α → β transition of β-lactoglobulin as evidenced by heteronuclear NMRJournal of Molecular Biology, 1998
- Trifluoroethanol Promotes Helix Formation by Destabilizing Backbone Exposure: Desolvation Rather than Native Hydrogen Bonding Defines the Kinetic Pathway of Dimeric Coiled Coil FoldingBiochemistry, 1998
- Group additive contributions to the alcohol-induced α-helix formation of melittin: implication for the mechanism of the alcohol effects on proteinsJournal of Molecular Biology, 1998
- Main-chain Dynamics of a Partially Folded Protein:15N NMR Relaxation Measurements of Hen Egg White Lysozyme Denatured in TrifluoroethanolJournal of Molecular Biology, 1996
- High Helical Propensity of the Peptide Fragments Derived from β-Lactoglobulin, a Predominantly β-sheet ProteinJournal of Molecular Biology, 1995
- Nonideality of Water-Hexafluoropropanol Mixtures as Studied by X-Ray Small Angle ScatteringBiochemical and Biophysical Research Communications, 1995
- Solution conformations and aggregational properties of synthetic amyloid β-peptides of Alzheimer's diseaseJournal of Molecular Biology, 1992
- Bee and Wasp VenomsScience, 1972
- Thermodynamics of protein denaturation. III. Denaturation of ribonuclease in water and in aqueous urea and aqueous ethanol mixturesJournal of the American Chemical Society, 1967
- DIELECTRIC CONSTANTS OF SOME ORGANIC SOLVENT-WATER MIXTURES AT VARIOUS TEMPERATURESJournal of the American Chemical Society, 1932