Thermodynamic consequences of the removal of a disulphide bridge from hen lysozyme
- 20 June 1992
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 225 (4), 939-943
- https://doi.org/10.1016/0022-2836(92)90094-z
Abstract
No abstract availableKeywords
This publication has 21 references indexed in Scilit:
- Spectroscopic, immunochemical, and thermodynamic properties of carboxymethyl(Cys6, Cys127)-hen egg white lysozymeProtein Journal, 1991
- Substantial increase of protein stability by multiple disulphide bondsNature, 1989
- Role of disulfide bonds in folding and secretion of human lysozyme in saccharomycescerevisiaeBiochemical and Biophysical Research Communications, 1988
- Disulphide bonds and protein stabilityBioEssays, 1988
- Protein folding kinetics from magnetization transfer nuclear magnetic resonanceBiochemistry, 1984
- Studies on the relationship of disulfide bonds to the formation and maintenance of secondary structure in chicken egg white lysozymeBiochemistry, 1982
- Intermediates in the refolding of reduced pancreatic trypsin inhibitorJournal of Molecular Biology, 1974
- A thermodynamic approach to the problem of stabilization of globular protein structure: A calorimetric studyJournal of Molecular Biology, 1974
- Oxidation of lysozyme by iodine: Identification and properties of an oxindolyl ester intermediate; evidence for participation of glutamic acid 35 in catalysisJournal of Molecular Biology, 1973
- Theory of Elastic Mechanisms in Fibrous ProteinsJournal of the American Chemical Society, 1956