Article
A buried polar residue in the hydrophobic interface of the coiled-coil peptide, GCN4-p1, plays a thermodynamic, not a kinetic role in folding.
Journal of molecular biology - 2 Aug 2002
Knappenberger Jane A, Smith Jennifer E, Thorpe Sarah H, Zitzewitz Jill A, Matthews C Robert
Abstract excerpt
The hydrophobic interfaces of coiled-coil proteins and peptides are typically interspersed with buried polar residues. These polar residues are known to be important for defining oligomeric specificity and chain orientation in coiled-coil formation; however, their effects on the folding/assembly reaction have not been investigated. The commonly studied 33-residue dimeric leucine zipper peptide, GCN4-p1, contains...
Topics
- Alanine
- Circular Dichroism
- DNA-Binding Proteins
- Dimerization
- Hydrophobic and Hydrophilic Interactions
- Kinetics
- Leucine Zippers
- Mutation
- Peptides
- Protein Denaturation
- Protein Folding
- Protein Kinases
- Protein Renaturation