Dissociation Kinetics of the GroEL−gp31 Chaperonin Complex Studied with Förster Resonance Energy Transfer-Reference-Cited by-同舟云学术

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Dissociation Kinetics of the GroEL−gp31 Chaperonin Complex Studied with Förster Resonance Energy Transfer

Published:2009-11-18 Issue:49 Volume:48 Page:11692-11698
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Calmat Stéphane¹²,Hendriks Johnny³,van Heerikhuizen Harm²,Schmidt Christoph F.⁴,van der Vies Saskia M.²,Peterman Erwin J. G.¹

Affiliation:

1. Department of Physics and Astronomy and Laser Centre, VU University, Amsterdam, The Netherlands

2. Department of Pathology, VU University Medical Center, Amsterdam, The Netherlands

3. Swammerdam Institute for Life Sciences, University of Amsterdam, Amsterdam, The Netherlands

4. Drittes Physikalisches Institut, Fakultät für Physik, Georg-August-Universität, Göttingen, Germany

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi9013962

Reference30 articles.

1. Proteome-wide Analysis of Chaperonin-Dependent Protein Folding in Escherichia coli

2. The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures

3. Location of a folding protein and shape changes in GroEL–GroES complexes imaged by cryo-electron microscopy

4. The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complex

5. GroEL−GroES-Mediated Protein Folding

Cited by 2 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Recombinant Expression and Purification of T4 Phage Hoc, Soc, gp23, gp24 Proteins in Native Conformations with Stability Studies;PLoS ONE;2012-07-13

2. Structure, Assembly, and DNA Packaging of the Bacteriophage T4 Head;Bacteriophages, Part A;2012

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