title: Protein folding and unfolding by Escherichia coli chaperones and chaperonins.
abstract: The folding of proteins from their initial unstructured state to their mature form has long been known to be promoted by other proteins known as chaperones and chaperonins. Recent biochemical and structural discoveries have provided dramatic insight into how these folding proteins work. This review will discuss these findings and suggest future experimental directions.
authors.affiliation: Departments of Microbiology and of Biochemistry and Molecular Biophysics, Institute of Cancer Research, Columbia University, New York, NY 10032, USA. gottesman@cuccfa.ccc.columbia.edu
authors.forename: M E
authors.initials: ME
authors.lastname: Gottesman
authors.forename: W A
authors.initials: WA
authors.lastname: Hendrickson
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D018833:Chaperonins / Q000737:chemistry / Q000378:metabolism*; D004926:Escherichia coli; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry* / Q000378:metabolism*; D011489:Protein Denaturation; D017510:Protein Folding; D013329:Structure-Activity Relationship
chemical_list: D001426:Bacterial Proteins; D018832:Molecular Chaperones; D018833:Chaperonins