The Antigenic Structure of Hen Egg-White Lysozyme: A Model for Disulfide-Containing Proteins
- 1 January 1977
- book chapter
- Published by Springer Nature
Abstract
No abstract availableThis publication has 102 references indexed in Scilit:
- Correlation of conformation and biological activity in lysozyme “loop” homologsJournal of Molecular Biology, 1974
- Enzymic and immunochemical properties of lysozyme—VIII. Modification of two carboxyl groyps and their role in the antigenic reactivityImmunochemistry, 1974
- Kinetic determinism of lysozyme folding at high temperaturesBiochemical and Biophysical Research Communications, 1974
- Environment and exposure to solvent of protein atoms. Lysozyme and insulinJournal of Molecular Biology, 1973
- Analysis of the circular dichroism of the lysozyme-α-lactalbumin group of proteinsBiochemistry, 1972
- A new nmr technique to study disulfide reduction: Comparison of lysozyme and α-lactalbuminBiochemical and Biophysical Research Communications, 1971
- An immunological approach to the structural relationship between hen egg-white lysozyme and bovine α-lactalbuminJournal of Molecular Biology, 1971
- A possible three-dimensional structure of bovine α-lactalbumin based on that of hen's egg-white lysozymeJournal of Molecular Biology, 1969
- Conversion of 3-nitrotyrosine to 3-aminotyrosine in peptides and proteinsBiochemical and Biophysical Research Communications, 1967
- Reaction of Anhydrous Formic Acid with Proteins1Journal of the American Chemical Society, 1959