Article
Tertiary structure-dependence of misfolding substitutions in loops of the maltose-binding protein.
Protein science : a publication of the Protein Society - 1 Oct 1998
Raffy S, Sassoon N, Hofnung M, Betton J M
Abstract excerpt
We previously identified and characterized amino acid substitutions in a loop connecting helix I to strand B, the alphaI/betaB loop, of the N-domain that are critical for in vivo folding of the maltose-binding protein (MalE31). The tertiary context-dependence of this mutation in MalE folding was...
Topics
- ATP-Binding Cassette Transporters
- Bacterial Proteins
- Carrier Proteins
- Escherichia coli
- Escherichia coli Proteins
- Fluorescence
- Guanidine
- Kinetics
- Maltose-Binding Proteins
- Monosaccharide Transport Proteins
- Mutagenesis, Site-Directed
- Mutation
- Periplasmic Binding Proteins
- Protein Folding
- Protein Structure, Secondary
- Protein Structure, Tertiary
- Scattering, Radiation