Domain-Specific Chaperone-Induced Expansion Is Required for β-Actin Folding: A Comparison of β-Actin Conformations upon Interactions with GroEL and Tail-less Complex Polypeptide 1 Ring Complex (TRiC)-Reference-Cited by-同舟云学术

Domain-Specific Chaperone-Induced Expansion Is Required for β-Actin Folding: A Comparison of β-Actin Conformations upon Interactions with GroEL and Tail-less Complex Polypeptide 1 Ring Complex (TRiC)

Published:2007-10-16 Issue:44 Volume:46 Page:12639-12647
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Villebeck Laila¹,Moparthi Satish Babu¹,Lindgren Mikael¹,Hammarström Per¹,Jonsson Bengt-Harald¹

Affiliation:

1. Divisions of Molecular Biotechnology and of Chemistry, IFM, Linköping University, 581 83 Linköping, Sweden, and Department of Physics, The Norwegian University of Science and Technology, 7491 Trondheim, Norway

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi700658n

Reference43 articles.

1. STRUCTURE AND FUNCTION IN GroEL-MEDIATED PROTEIN FOLDING

2. Group II chaperonins: new TRiC(k)s and turns of a protein folding machine

3. Structure and function of a protein folding machine: the eukaryotic cytosolic chaperonin CCT

4. The thermosome: archetype of group II chaperonins

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