Karamanos, TK orcid.org/0000-0003-2297-540X and Clore, GM (2022) Large Chaperone Complexes Through the Lens of Nuclear Magnetic Resonance Spectroscopy. Annual Review of Biophysics. ISSN 1936-122X
Abstract
Molecular chaperones are the guardians of the proteome inside the cell. Chaperones recognize and bind unfolded or misfolded substrates, thereby preventing further aggregation; promoting correct protein folding; and, in some instances, even disaggregating already formed aggregates. Chaperones perform their function by means of an array of weak protein–protein interactions that take place over a wide range of timescales and are therefore invisible to structural techniques dependent upon the availability of highly homogeneous samples. Nuclear magnetic resonance (NMR) spectroscopy, however, is ideally suited to study dynamic, rapidly interconverting conformational states and protein–protein interactions in solution, even if these involve a high-molecular-weight component. In this review, we give a brief overview of the principles used by chaperones to bind their client proteins and describe NMR methods that have emerged as valuable tools to probe chaperone–substrate and chaperone–chaperone interactions. We then focus on a few systems for which the application of these methods has greatly increased our understanding of the mechanisms underlying chaperone functions.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Keywords: | chaperones, chaperone–substrate interactions, molecular recognition, NMR spectroscopy, excited transient states, exchange dynamics, kinetics |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 09 Mar 2022 14:43 |
Last Modified: | 10 Mar 2022 09:38 |
Status: | Published online |
Publisher: | Annual Reviews |
Identification Number: | 10.1146/annurev-biophys-090921-120150 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:184464 |