Article
Indication of possible post-translational formation of disulphide bonds in the beta-sheet domain of human lysozyme.
The Biochemical journal - 1 Jun 1993
Kanaya E, Ishihara K, Tsunasawa S, Nokihara K, Kikuchi M
Abstract excerpt
Lysozyme has two distinct folding domains, and in most molecules the alpha-helical domain folds more quickly than the beta-sheet domain in vitro [Radford, Dobson and Evans (1992) Nature (London) 358, 302-307]. In order to investigate the relationship between the formation of disulphide bonds and...
Topics
- Amino Acid Sequence
- Base Sequence
- Chromatography, High Pressure Liquid
- Cloning, Molecular
- Cysteine
- DNA, Single-Stranded
- Disulfides
- Humans
- Molecular Sequence Data
- Muramidase
- Mutation
- Peptide Mapping
- Protein Folding
- Protein Processing, Post-Translational
- Saccharomyces cerevisiae
- Sequence Alignment