Article
Interaction of SecB with intermediates along the folding pathway of maltose-binding protein.
Protein science : a publication of the Protein Society - 1 Jun 1995
Diamond D L, Strobel S, Chun S Y, Randall L L
Abstract excerpt
SecB, a molecular chaperone involved in protein export in Escherichia coli, displays the remarkable ability to selectively bind many different polypeptide ligands whose only common feature is that of being nonnative. The selectivity is explained in part by a kinetic partitioning between the foldi...
Topics
- ATP-Binding Cassette Transporters
- Bacterial Proteins
- Carrier Proteins
- Dose-Response Relationship, Drug
- Escherichia coli
- Escherichia coli Proteins
- Guanidine
- Guanidines
- Kinetics
- Maltose-Binding Proteins
- Molecular Chaperones
- Monosaccharide Transport Proteins
- Mutation
- Protein Conformation
- Protein Denaturation
- Protein Folding