Article
A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants.
Science (New York, N.Y.) - 26 Nov 1993
Harbury P B, Zhang T, Kim P S, Alber T
Abstract excerpt
Coiled-coil sequences in proteins consist of heptad repeats containing two characteristic hydrophobic positions. The role of these buried hydrophobic residues in determining the structures of coiled coils was investigated by studying mutants of the GCN4 leucine zipper. When sets of buried residue...
Topics
- Amino Acid Sequence
- Crystallography, X-Ray
- DNA-Binding Proteins
- Fungal Proteins
- Hydrogen Bonding
- Leucine Zippers
- Molecular Sequence Data
- Mutation
- Protein Conformation
- Protein Kinases
- Protein Structure, Secondary
- Saccharomyces cerevisiae Proteins