Article
Single-site mutations induce 3D domain swapping in the B1 domain of protein L from Peptostreptococcus magnus.
Structure (London, England : 1993) - 1 Nov 2001
O'Neill J W, Kim D E, Johnsen K, Baker D, Zhang K Y
Abstract excerpt
BACKGROUND: Thermodynamic and kinetic studies of the Protein L B1 domain (Ppl) suggest a folding pathway in which, during the folding transition, the first beta hairpin is formed while the second beta hairpin and the alpha helix are largely unstructured. The same mutations in the two beta turns have opposite effects on the folding and unfolding rates. Three of the four residues composing the second beta turn in...
Topics
- Bacterial Proteins
- Crystallography
- Dimerization
- Hydrogen Bonding
- Kinetics
- Models, Chemical
- Models, Molecular
- Mutation
- Peptostreptococcus
- Protein Folding
- Protein Structure, Quaternary