Isolation and biochemical characterization of highly purified Escherichia coli molecular chaperone Cpn60 (GroEL) by affinity chromatography and urea-induced monomerization-Reference-Cited by-同舟云学术

Isolation and biochemical characterization of highly purified Escherichia coli molecular chaperone Cpn60 (GroEL) by affinity chromatography and urea-induced monomerization

Published:1995-09 Issue:1 Volume:1252 Page:69-78
ISSN:0167-4838
Container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology

Author:

Blennow Andreas,Surin Brian P,Ehring Hanno,McLennan Neil F,Spangfort Michael D

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Structural Biology

Reference24 articles.

1. MOLECULAR CHAPERONES

2. Homologous plant and bacterial proteins chaperone oligomeric protein assembly

3. GroEL/ES-mediated refolding of human carbonic anhydrase II: role of N-terminal helices as recognition motifs for GroEL

4. (Mg–ATP)-dependent self-assembly of molecular chaperone GroEL

5. Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity.

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