Journal
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
Volume 48, Issue 4, Pages 611-617Publisher
WILEY
DOI: 10.1002/prot.10180
Keywords
nested allostery; cooperativity; GroES; chaperonins; molecular chaperones; protein folding
Categories
Ask authors/readers for more resources
An interesting example of an allosteric protein is the chaperonin GroEL. It undergoes adenosine 5'-triphosphate-induced conformational changes that are reflected in binding of adenosine 5'-triphosphate with positive cooperativity within rings and negative cooperativity between rings. Herein, correlated mutations in chaperonins are analyzed to unravel routes of allosteric communication in GroEL and in its complex with its cochaperonin GroES. It is shown that analysis of correlated mutations in the chaperonin family can provide information about pathways of allosteric communication within GroEL and between GroEL and GroES. The results are discussed in the context of available structural, genetic, and biochemical data concerning short- and long-range interactions in the GroE system. Proteins 2002;48:611-617. (C) 2002 Wiley-Liss, Inc.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available