Chaperone-assisted protein folding Journal Article

  


Authors: Martin, J.; Ulrich Hartl, F.
Article Title: Chaperone-assisted protein folding
Abstract: Molecular chaperones of the Hsp70 and chaperonin families are basic constituents of the cellular machinery that mediates protein folding. Recent functional and structural studies corroborate existing models for the mechanism of these components. Highlights of the past year include the X-ray crystallographic analysis of the peptide-binding domain of the Escherichia coli Hsp70 homolog, DnaK, the direct demonstration of protein folding in the central cavity of the chaperonin GroEL, and the visualization of conformational changes in GroEL during the chaperonin folding cycle.
Keywords: review; protein conformation; protein domain; protein; bacteria (microorganisms); bacterial protein; escherichia coli; heat shock protein 70; conformational transition; protein folding; protein structure; x ray crystallography; molecular model; hsp70 heat-shock proteins; chaperone; chaperonins; priority journal; chaperonin
Journal Title: Current Opinion in Structural Biology
Volume: 7
Issue: 1
ISSN: 0959-440X
Publisher: Elsevier Inc.  
Date Published: 1997-02-01
Start Page: 41
End Page: 52
Language: English
DOI: 10.1016/s0959-440x(97)80006-1
PUBMED: 9032064
PROVIDER: scopus
DOI/URL:

https://www.scopus.com/inward/record.uri?eid=2-s2.0-0343488499&doi=10.1016%2fS0959-440X%2897%2980006-1&partnerID=40&md5=5af52e2c06ad60bbeedc3e5948ee7582
Notes: Review -- Export Date: 17 March 2017 -- Source: Scopus
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