NMR Solution Structure of the 21 kDa Chaperone Protein DnaK Substrate Binding Domain: A Preview of Chaperone−Protein Interaction-Reference-Cited by-同舟云学术

NMR Solution Structure of the 21 kDa Chaperone Protein DnaK Substrate Binding Domain: A Preview of Chaperone−Protein Interaction

Published:1998-05-14 Issue:22 Volume:37 Page:7929-7940
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Wang Hong¹,Kurochkin Alexander V.¹,Pang Yuxi¹,Hu Weidong¹,Flynn Gregory C.¹,Zuiderweg Erik R. P.¹

Affiliation:

1. Biophysics Research Division, Department of Biological Chemistry, and Department of Chemistry, The University of Michigan, 930 North University Avenue, Ann Arbor, Michigan 48109, and Institute of Molecular Biology, University of Oregon, Eugene Oregon

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi9800855

Reference69 articles.

1. Genetic analysis of two genes, dnaJ and dnaK, necessary for Escherichia coli and bacteriophage lambda DNA replication

2. MOLECULAR CHAPERONE FUNCTIONS OF HEAT-SHOCK PROTEINS

3. Heat shock proteins: molecular chaperones of protein biogenesis

4. Chaperone-assisted protein folding

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