Accession Number : ADP008361

Title :   Recognition of Peptides by the E. Coli Molecular Chaperones, GroEL and DnaK,

Corporate Author : TEXAS UNIV SOUTHWESTERN MEDICAL SCHOOL AT DALLAS

Personal Author(s) : Landry, Samuel J. ; Gierasch, Lila M.

Report Date : 1992

Pagination or Media Count : 3

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.

Descriptors :   *PEPTIDES, *ESCHERICHIA COLI, PROTEINS, IN VIVO ANALYSIS, CHAIN REACTIONS, STRESS(PHYSIOLOGY), HEAT STRESS(PHYSIOLOGY), HELIXES.

Subject Categories : Biochemistry
      Microbiology
      Pharmacology

Distribution Statement : APPROVED FOR PUBLIC RELEASE