Protein folding and unfolding by Escherichia coli chaperones and chaperonins.
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.
Gottesman
M E
ME
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
Hendrickson
W A
WA
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
D001426:Bacterial Proteins; D018832:Molecular Chaperones; D018833:Chaperonins