Article
Structure of a thermostable disulfide-bridge mutant of phage T4 lysozyme shows that an engineered cross-link in a flexible region does not increase the rigidity of the folded protein.
Biochemistry - 13 Mar 1990
Pjura P E, Matsumura M, Wozniak J A, Matthews B W
Abstract excerpt
A disulfide bond introduced between amino acid positions 9 and 164 in phage T4 lysozyme has been shown to significantly increase the stability of the enzyme toward thermal denaturation [Matsumura, M., Becktel, W.J., Levitt, M., & Matthews, B. W. (1989) Proc. Natl. Acad. Sci. U.S.A. 86, 6562-6566]. To elucidate the structural features of the engineered disulfide, the crystal structure of the disulfide mutant has...
Topics
- Cross-Linking Reagents
- Disulfides
- Molecular Sequence Data
- Muramidase
- Mutation
- Protein Conformation
- Stereoisomerism
- T-Phages
- Temperature