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

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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
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PubType: Academic Journal
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  Data: <searchLink fieldCode="JN" term="%22Nature%22">Nature</searchLink>. 7/4/1991, Vol. 352 Issue 6330, p36. 7p. 6 Black and White Photographs, 1 Diagram, 1 Chart, 14 Graphs.
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  Data: 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.
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        Value: 10.1038/352036a0
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      – Code: eng
        Text: English
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        PageCount: 7
        StartPage: 36
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              Text: 7/4/1991
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              Y: 1991
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