Tandem Mass Spectrometry of Intact GroEL−Substrate Complexes Reveals Substrate-Specific Conformational Changes in the trans Ring-Reference-Cited by-同舟云学术

Tandem Mass Spectrometry of Intact GroEL−Substrate Complexes Reveals Substrate-Specific Conformational Changes in the trans Ring

Published:2006-03-16 Issue:14 Volume:128 Page:4694-4702
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

van Duijn Esther¹,Simmons Douglas A.¹,van den Heuvel Robert H. H.¹,Bakkes Patrick J.¹,van Heerikhuizen Harm¹,Heeren Ron M. A.¹,Robinson Carol V.¹,van der Vies Saskia M.¹,Heck Albert J. R.¹

Affiliation:

1. Contribution from the Department of Biomolecular Mass Spectrometry, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, The Netherlands, Department of Biochemistry and Molecular Biology, Faculty of Sciences, Vrije Universiteit, Amsterdam, The Netherlands, Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, United Kingdom, and FOM Institute for Atomic and Molecular Physics (AMOLF), The Netherlands

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja056756l

Reference50 articles.

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

2. Identification of in vivo substrates of the chaperonin GroEL

3. ATP-Bound States of GroEL Captured by Cryo-Electron Microscopy

4. The substrate recognition mechanisms in chaperonins

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