Protein Tethering for Folding Studies

Moayed, Fatemeh; Wijk, Roeland J. van; Minde, David-Paul; Tans, Sander J.

doi:10.1007/978-1-4939-7271-5_3

Cited by 2 publications

(1 citation statement)

References 16 publications

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“…Oligonucleotides were then hybridized with an overhang presented in longer DNA handles [125]. Other chemical couplings have been developed (reviewed, for example, here [126]), including click chemistry, unnatural amino acids and others [127][128][129][130]. Using different coupling strategies enables the attachment of linkers of different mechanical elastic properties, which may affect the quality of the signal.…”

Section: Advances In Single-molecule Force Spectroscopy Of Proteinsmentioning

confidence: 99%

Single-molecule mechanical studies of chaperones and their clients

Rief

2022

Biophysics Reviews

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Single-molecule force spectroscopy provides access to the mechanics of biomolecules. Recently, magnetic and laser optical tweezers were applied in the studies of chaperones and their interaction with protein clients. Various aspects of the chaperone–client interactions can be revealed based on the mechanical probing strategies. First, when a chaperone is probed under load, one can examine the inner workings of the chaperone while it interacts with and works on the client protein. Second, when protein clients are probed under load, the action of chaperones on folding clients can be studied in great detail. Such client folding studies have given direct access to observing actions of chaperones in real-time, like foldase, unfoldase, and holdase activity. In this review, we introduce the various single molecule mechanical techniques and summarize recent single molecule mechanical studies on heat shock proteins, chaperone-mediated folding on the ribosome, SNARE folding, and studies of chaperones involved in the folding of membrane proteins. An outlook on significant future developments is given.

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Section: Advances In Single-molecule Force Spectroscopy Of Proteinsmentioning

confidence: 99%

Single-molecule mechanical studies of chaperones and their clients

Rief

2022

Biophysics Reviews

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From folding to function: complex macromolecular reactions unraveled one-by-one with optical tweezers

Heidarsson

Cecconi

2021

Essays in Biochemistry

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Single-molecule manipulation with optical tweezers has uncovered macromolecular behaviour hidden to other experimental techniques. Recent instrumental improvements have made it possible to expand the range of systems accessible to optical tweezers. Beyond focusing on the folding and structural changes of isolated single molecules, optical tweezers studies have evolved into unraveling the basic principles of complex molecular processes such as co-translational folding on the ribosome, kinase activation dynamics, ligand–receptor binding, chaperone-assisted protein folding, and even dynamics of intrinsically disordered proteins (IDPs). In this mini-review, we illustrate the methodological principles of optical tweezers before highlighting recent advances in studying complex protein conformational dynamics – from protein synthesis to physiological function – as well as emerging future issues that are beginning to be addressed with novel approaches.

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Protein Tethering for Folding Studies

Cited by 2 publications

References 16 publications

Single-molecule mechanical studies of chaperones and their clients

Single-molecule mechanical studies of chaperones and their clients

From folding to function: complex macromolecular reactions unraveled one-by-one with optical tweezers

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