Article
Alpha-helix stability and the native state of myoglobin.
Biochemistry - 30 Nov 1993
Lin L, Pinker R J, Kallenbach N R
Abstract excerpt
Native proteins fold to form structures that contain secondary-structure regular patterns in the peptide backbone, such as alpha-helix, beta-structure, and turns with high frequency. The role of this secondary structure in stabilizing the native folded state is presently unclear. Alanine substitutions at helical sites in myoglobin show no correlation with the helical propensity of the side chains involved. In an...
Topics
- Mutagenesis, Site-Directed
- Mutation
- Myoglobin
- Protein Conformation
- Protein Denaturation
- Protein Structure, Secondary
- Recombinant Proteins
- Surface Properties
- Urea