Article
Probing the stability of a partly folded apomyoglobin intermediate by site-directed mutagenesis.
Biochemistry - 30 Apr 1991
Hughson F M, Barrick D, Baldwin R L
Abstract excerpt
A partly folded form (I) of apomyoglobin has an alpha-helix content of about 35%; in an earlier study, hydrogen exchange revealed that the A, G, and H helices are folded, while much of the rest of the protein is not [Hughson, F. M., Wright, P. E., & Baldwin, R. L. (1990) Science 249, 1544-1548]. Because A, G, and H form a compact subdomain in native myoglobin, we proposed that nativelike packing interactions...
Topics
- Amino Acid Sequence
- Apoproteins
- Circular Dichroism
- Hydrogen-Ion Concentration
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Mutation
- Myoglobin
- Plasmids
- Protein Conformation
- Protein Denaturation