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Science 12 January 1996:
Vol. 271. no. 5246, p. 161
DOI: 10.1126/science.271.5246.161
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Perspectives

Mark Mayhew, F. Ulrich Hartl

The crystal structure of the chaparonin GroES, which together with GroEL assists in the folding of many proteins in Escherichia coli, is reported in this issue of Science by Mande et al. (p. 203). In this Perspective, M. Mayhew and F. U. Hartl discuss the implications of the new structure for the function of the GroEL:GroES complex.

The authors are in the Howard Hughes Medical Institute and Cellular Biochemistry and Biophysics Program, Memorial Sloan Kettering Cancer Center, New York, NY 10021, USA.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
GroEL/GroES Promote Dissociation/Reassociation Cycles of a Heterodimeric Intermediate during alpha 2beta 2 Protein Assembly. ITERATIVE ANNEALING AT THE QUATERNARY STRUCTURE LEVEL.
R. M. Wynn, J.-L. Song, and D. T. Chuang (2000)
J. Biol. Chem. 275, 2786-2794
   Abstract »    Full Text »    PDF »
GroEL/GroES-dependent Reconstitution of alpha 2beta 2 Tetramers of Human Mitochondrial Branched Chain alpha -Ketoacid Decarboxylase. OBLIGATORY INTERACTION OF CHAPERONINS WITH AN alpha beta DIMERIC INTERMEDIATE.
J. L. Chuang, R. M. Wynn, J.-L. Song, and D. T. Chuang (1999)
J. Biol. Chem. 274, 10395-10404
   Abstract »    Full Text »    PDF »


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Science. ISSN 0036-8075 (print), 1095-9203 (online)