The Dynamic Conformational Cycle of the Group I Chaperonin C-Termini Revealed via Molecular Dynamics Simulation
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Title
The Dynamic Conformational Cycle of the Group I Chaperonin C-Termini Revealed via Molecular Dynamics Simulation
Authors
Keywords
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Journal
PLoS One
Volume 10, Issue 3, Pages e0117724
Publisher
Public Library of Science (PLoS)
Online
2015-03-31
DOI
10.1371/journal.pone.0117724
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- (2012) Daniel K. Clare et al. CELL
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- (2012) Vincent A. Voelz et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
- The Molecular Architecture of the Eukaryotic Chaperonin TRiC/CCT
- (2012) Alexander Leitner et al. STRUCTURE
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- (2011) Haibin Luo et al. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
- Dual Action of ATP Hydrolysis Couples Lid Closure to Substrate Release into the Group II Chaperonin Chamber
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- Double mutant MBP refolds at same rate in free solution as inside the GroEL/GroES chaperonin chamber when aggregation in free solution is prevented
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- (2011) F. Ulrich Hartl et al. NATURE
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- (2010) P. Emsley et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- Crystal Structures of a Group II Chaperonin Reveal the Open and Closed States Associated with the Protein Folding Cycle
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- (2010) H. Hofmann et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
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