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  A mobile loop order-disorder transition modulates the speed of chaperonin cycling

Shewmaker, F., Kerner, M. J., Hayer-Hartl, M., Klein, G., Georgopoulos, C., & Landry, S. J. (2004). A mobile loop order-disorder transition modulates the speed of chaperonin cycling. Protein Science, 13(8), 2139-2148.

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Genre: Journal Article
Alternative Title : Protein Sci.

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 Creators:
Shewmaker, F., Author
Kerner, M. J.1, Author           
Hayer-Hartl, M.2, Author           
Klein, G., Author
Georgopoulos, C., Author
Landry, S. J., Author
Affiliations:
1Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565152              
2Hayer-Hartl, Manajit / Chaperonin-assisted Protein Folding, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565153              

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Free keywords: nuclear magnetic resonance; surface plasmon resonance; ATP hydrolysis; folding funnel; allele-specific; genetic interaction; intrinsically unstructured protein
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Language(s): eng - English
 Dates: 2004-08
 Publication Status: Issued
 Pages: -
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 214697
ISI: 000222928800016
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Title: Protein Science
  Alternative Title : Protein Sci.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 13 (8) Sequence Number: - Start / End Page: 2139 - 2148 Identifier: ISSN: 0961-8368