Article
The structure of Fis mutant Pro61Ala illustrates that the kink within the long alpha-helix is not due to the presence of the proline residue.
The Journal of biological chemistry - 18 Nov 1994
Yuan H S, Wang S S, Yang W Z, Finkel S E, Johnson R C
Abstract excerpt
The influence of proline on bending of the alpha-helix was investigated by replacement of the proline residue located in the middle of the long alpha-helix of the Fis protein with alanine, serine, or leucine. Each of the three substitutions folded into a stable protein with the same or higher mel...
Topics
- Alanine
- Base Sequence
- Carrier Proteins
- DNA-Binding Proteins
- Factor For Inversion Stimulation Protein
- Integration Host Factors
- Molecular Sequence Data
- Mutation
- Oligodeoxyribonucleotides
- Proline
- Protein Conformation