Article
Global suppression of protein folding defects and inclusion body formation.
Science (New York, N.Y.) - 5 Jul 1991
Mitraki A, Fane B, Haase-Pettingell C, Sturtevant J, King J
Abstract excerpt
Amino acid substitutions at a site in the center of the bacteriophage protein P22 tailspike polypeptide chain suppress temperature-sensitive folding mutations at many sites throughout the chain. Characterization of the intracellular folding and chain assembly process reveals that the suppressors act in the folding pathway, inhibiting the aggregation of an early folding intermediate into the kinetically trapped...
Topics
- Amino Acid Sequence
- Coliphages
- DNA Mutational Analysis
- Electrophoresis, Polyacrylamide Gel
- Gene Expression Regulation
- Inclusion Bodies
- Molecular Sequence Data
- Mutation
- Protein Conformation
- Viral Proteins
- Viral Tail Proteins