Recognition of Peptides by the E. Coli Molecular Chaperones, GroEL and DnaK,
Abstract
Recent evidence indicates that protein folding in vivo is facilitated by a group of factors collectively known as molecular chaperones. The functions of chaperones may include prevention of aggregation of nascent chains, avoidance of incorrectly folded states, prolongation of the lifetime of incompletely folded chains to enable their translocation across membranes, and enhancement of assembly of oligomeric proteins.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jan 01, 1992
- Accession Number
- ADP008361
Entities
People
- Lila M. Gierasch
- Samuel J. Landry
Organizations
- University of Texas Southwestern Medical Center