Probing the Sequence of Conformationally Induced Polarity Changes in the Molecular Chaperonin GroEL with Fluorescence Spectroscopy-Reference-Cited by-同舟云学术

Probing the Sequence of Conformationally Induced Polarity Changes in the Molecular Chaperonin GroEL with Fluorescence Spectroscopy

Published:2005-12-01 Issue:51 Volume:109 Page:24517-24525
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Kim So Yeon¹,Semyonov Alexander N.¹,Twieg Robert J.¹,Horwich Arthur L.¹,Frydman Judith¹,Moerner W. E.¹

Affiliation:

1. Department of Chemistry, Stanford University, Stanford, California 94305, Department of Chemistry, Kent State University, Kent, Ohio 44242, Howard Hughes Medical Institute and Yale University School of Medicine, New Haven, Connecticut 06510, and Department of Biological Sciences, Stanford University, Stanford, California 94305

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/jp0534232

Reference65 articles.

1. Folding of Newly Translated Proteins In Vivo: The Role of Molecular Chaperones

2. Molecular chaperones in cellular protein folding

3. The Hsp70 and Hsp60 Chaperone Machines

4. STRUCTURE AND FUNCTION IN GroEL-MEDIATED PROTEIN FOLDING

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