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Nature Structural Biology  9, 406 - 408 (2002)
doi:10.1038/nsb0602-406

A new twist for an Hsp70 chaperone

Joanna F. Swain1 & Lila M. Gierasch2

1  Joanna F. Swain is in the Department of Biochemistry Molecular Biology at the University of Massachusetts, Amherst, Massachusetts 01003, USA. feltham@nsm.umass.edu

2  Lila M. Gierasch is in the Department of Biochemistry & Molecular Biology and the Department of Chemistry at the University of Massachusetts, Amherst, Massachusetts 01003, USA.

A new study has demonstrated that the E. coli Hsp70, DnaK, can catalyze cis-trans isomerization of non-prolyl peptide bonds.

MORE ARTICLES LIKE THIS
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REFERENCE
Peptidyl Prolyl cis – trans Isomerases
Nature Encyclopaedia of Life Sciences
Chaperones, Chaperonin and Heat-Shock Proteins
Nature Encyclopaedia of Life Sciences
 See all 3 matches for Reference

NEWS AND VIEWS
Proline not the only culprit?
Nature Structural Biology News and Views (01 May 2001)

RESEARCH
The hsp70 chaperone DnaK is a secondary amide peptide bond cis-trans isomerase
Nature Structural Biology Letters (01 Jun 2002)
Nonprolyl cis peptide bonds in unfolded proteins cause complex folding kinetics
Nature Structural Biology Article (01 May 2001)

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Nature Structural & Molecular Biology
ISSN: 1545-9993
EISSN: 1545-9985
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