Intrinsic unfoldase/foldase activity of the chaperonin GroEL directly demonstrated using multinuclear relaxation-based NMR
Published 2015 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
Intrinsic unfoldase/foldase activity of the chaperonin GroEL directly demonstrated using multinuclear relaxation-based NMR
Authors
Keywords
-
Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 112, Issue 29, Pages 8817-8823
Publisher
Proceedings of the National Academy of Sciences
Online
2015-06-30
DOI
10.1073/pnas.1510083112
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- Visualizing transient dark states by NMR spectroscopy
- (2015) Nicholas J. Anthis et al. QUARTERLY REVIEWS OF BIOPHYSICS
- Characterizing Methyl-Bearing Side Chain Contacts and Dynamics Mediating Amyloid β Protofibril Interactions Using13Cmethyl-DEST and Lifetime Line Broadening
- (2014) Nicolas L. Fawzi et al. ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
- Chemical exchange in biomacromolecules: Past, present, and future
- (2014) Arthur G. Palmer JOURNAL OF MAGNETIC RESONANCE
- Measuring how much work the chaperone GroEL can do
- (2013) N. C. Corsepius et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- GroEL and CCT are catalytic unfoldases mediating out-of-cage polypeptide refolding without ATP
- (2013) S. Priya et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Probing the transient dark state of substrate binding to GroEL by relaxation-based solution NMR
- (2013) D. S. Libich et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- A 2D 13C-CEST experiment for studying slowly exchanging protein systems using methyl probes: an application to protein folding
- (2012) Guillaume Bouvignies et al. JOURNAL OF BIOMOLECULAR NMR
- Measurement of 15N relaxation rates in perdeuterated proteins by TROSY-based methods
- (2012) Nils-Alexander Lakomek et al. JOURNAL OF BIOMOLECULAR NMR
- Probing exchange kinetics and atomic resolution dynamics in high-molecular-weight complexes using dark-state exchange saturation transfer NMR spectroscopy
- (2012) Nicolas L Fawzi et al. Nature Protocols
- Structure of an Intermediate State in Protein Folding and Aggregation
- (2012) P. Neudecker et al. SCIENCE
- Methods to determine slow diffusion coefficients of biomolecules. Applications to Engrailed 2, a partially disordered protein
- (2011) Rafal Augustyniak et al. JOURNAL OF BIOMOLECULAR NMR
- Atomic-resolution dynamics on the surface of amyloid-β protofibrils probed by solution NMR
- (2011) Nicolas L. Fawzi et al. NATURE
- Molecular chaperones in protein folding and proteostasis
- (2011) F. Ulrich Hartl et al. NATURE
- Kinetics of Amyloid β Monomer-to-Oligomer Exchange by NMR Relaxation
- (2010) Nicolas L. Fawzi et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
- Chaperonin-mediated protein folding: using a central cavity to kinetically assist polypeptide chain folding
- (2009) Arthur L. Horwich et al. QUARTERLY REVIEWS OF BIOPHYSICS
- Monitoring Protein Conformation along the Pathway of Chaperonin-Assisted Folding
- (2008) Shruti Sharma et al. CELL
- Chaperone machines in action
- (2008) Helen R Saibil CURRENT OPINION IN STRUCTURAL BIOLOGY
- GroEL stimulates protein folding through forced unfolding
- (2008) Zong Lin et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Setting the chaperonin timer: A two-stroke, two-speed, protein machine
- (2008) J. P. Grason et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- An Improved15N Relaxation Dispersion Experiment for the Measurement of Millisecond Time-Scale Dynamics in Proteins†
- (2007) D. Flemming Hansen et al. JOURNAL OF PHYSICAL CHEMISTRY B
Publish scientific posters with Peeref
Peeref publishes scientific posters from all research disciplines. Our Diamond Open Access policy means free access to content and no publication fees for authors.
Learn MoreAsk a Question. Answer a Question.
Quickly pose questions to the entire community. Debate answers and get clarity on the most important issues facing researchers.
Get Started