Chaperonin-mediated protein folding at the surface of groEL through a `molten globule'-like...

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Bibliographic Details
Title: Chaperonin-mediated protein folding at the surface of groEL through a `molten globule'-like...
Authors: Martin, J., Langer, T.
Source: Nature. 7/4/1991, Vol. 352 Issue 6330, p36. 7p. 6 Black and White Photographs, 1 Diagram, 1 Chart, 14 Graphs.
Subjects: Protein research
Abstract: Presents the reproduction of the chaperonin-dependent folding of two monomeric enzymes, dihydrofolate reductase (DHFR) and rhodanese, using the groEL and groES proteins of `Escherichia coli.' GroEL stabilizing a `molten globule'-like state; DHFRfolding through a more compact intermediate; GroES and folding at the groEL surface; ATP requirement at folding.
Database: Engineering Source
Description
Abstract:Presents the reproduction of the chaperonin-dependent folding of two monomeric enzymes, dihydrofolate reductase (DHFR) and rhodanese, using the groEL and groES proteins of `Escherichia coli.' GroEL stabilizing a `molten globule'-like state; DHFRfolding through a more compact intermediate; GroES and folding at the groEL surface; ATP requirement at folding.
ISSN:00280836
DOI:10.1038/352036a0