---
_id: '14847'
abstract:
- lang: eng
text: Understanding the mechanisms of chaperones at the atomic level generally requires
producing chaperone–client complexes in vitro. This task comes with significant
challenges, because one needs to find conditions in which the client protein is
presented to the chaperone in a state that binds and at the same time avoid the
pitfalls of protein aggregation that are often inherent to such states. The strategy
differs significantly for different client proteins and chaperones, but there
are common underlying principles. Here, we discuss these principles and deduce
the strategies that can be successfully applied for different chaperone–client
complexes. We review successful biochemical strategies applied to making the client
protein “binding competent” and illustrate the different strategies with examples
of recent biophysical and biochemical studies.
alternative_title:
- New Developments in NMR
article_processing_charge: No
author:
- first_name: I.
full_name: Sučec, I.
last_name: Sučec
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: 'Sučec I, Schanda P. Preparing Chaperone–Client Protein Complexes for Biophysical
and Structural Studies. In: Hiller S, Liu M, He L, eds. Biophysics of Molecular
Chaperones. Vol 29. Royal Society of Chemistry; 2023:136-161. doi:10.1039/bk9781839165986-00136'
apa: Sučec, I., & Schanda, P. (2023). Preparing Chaperone–Client Protein Complexes
for Biophysical and Structural Studies. In S. Hiller, M. Liu, & L. He (Eds.),
Biophysics of Molecular Chaperones (Vol. 29, pp. 136–161). Royal Society
of Chemistry. https://doi.org/10.1039/bk9781839165986-00136
chicago: Sučec, I., and Paul Schanda. “Preparing Chaperone–Client Protein Complexes
for Biophysical and Structural Studies.” In Biophysics of Molecular Chaperones,
edited by Sebastian Hiller, Maili Liu, and Lichun He, 29:136–61. Royal Society
of Chemistry, 2023. https://doi.org/10.1039/bk9781839165986-00136.
ieee: I. Sučec and P. Schanda, “Preparing Chaperone–Client Protein Complexes for
Biophysical and Structural Studies,” in Biophysics of Molecular Chaperones,
vol. 29, S. Hiller, M. Liu, and L. He, Eds. Royal Society of Chemistry, 2023,
pp. 136–161.
ista: 'Sučec I, Schanda P. 2023.Preparing Chaperone–Client Protein Complexes for
Biophysical and Structural Studies. In: Biophysics of Molecular Chaperones. New
Developments in NMR, vol. 29, 136–161.'
mla: Sučec, I., and Paul Schanda. “Preparing Chaperone–Client Protein Complexes
for Biophysical and Structural Studies.” Biophysics of Molecular Chaperones,
edited by Sebastian Hiller et al., vol. 29, Royal Society of Chemistry, 2023,
pp. 136–61, doi:10.1039/bk9781839165986-00136.
short: I. Sučec, P. Schanda, in:, S. Hiller, M. Liu, L. He (Eds.), Biophysics of
Molecular Chaperones, Royal Society of Chemistry, 2023, pp. 136–161.
date_created: 2024-01-22T08:04:57Z
date_published: 2023-11-01T00:00:00Z
date_updated: 2024-01-23T11:50:10Z
day: '01'
department:
- _id: PaSc
doi: 10.1039/bk9781839165986-00136
editor:
- first_name: Sebastian
full_name: Hiller, Sebastian
last_name: Hiller
- first_name: Maili
full_name: Liu, Maili
last_name: Liu
- first_name: Lichun
full_name: He, Lichun
last_name: He
intvolume: ' 29'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.26434/chemrxiv-2023-rpn28
month: '11'
oa: 1
oa_version: Preprint
page: 136-161
publication: Biophysics of Molecular Chaperones
publication_identifier:
eisbn:
- '9781839165993'
isbn:
- '9781839162824'
publication_status: published
publisher: Royal Society of Chemistry
quality_controlled: '1'
status: public
title: Preparing Chaperone–Client Protein Complexes for Biophysical and Structural
Studies
type: book_chapter
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 29
year: '2023'
...
---
_id: '14848'
abstract:
- lang: eng
text: Regulating protein states is considered the core function of chaperones. However,
despite their importance to all major cellular processes, the conformational changes
that chaperones impart on polypeptide chains are difficult to study directly due
to their heterogeneous, dynamic, and multi-step nature. Here, we review recent
advances towards this aim using single-molecule manipulation methods, which are
rapidly revealing new mechanisms of conformational control and helping to define
a different perspective on the chaperone function.
alternative_title:
- New Developments in NMR
article_processing_charge: No
author:
- first_name: F.
full_name: Wruck, F.
last_name: Wruck
- first_name: Mario
full_name: Avellaneda Sarrió, Mario
id: DC4BA84C-56E6-11EA-AD5D-348C3DDC885E
last_name: Avellaneda Sarrió
orcid: 0000-0001-6406-524X
- first_name: M. M.
full_name: Naqvi, M. M.
last_name: Naqvi
- first_name: E. J.
full_name: Koers, E. J.
last_name: Koers
- first_name: K.
full_name: Till, K.
last_name: Till
- first_name: L.
full_name: Gross, L.
last_name: Gross
- first_name: F.
full_name: Moayed, F.
last_name: Moayed
- first_name: A.
full_name: Roland, A.
last_name: Roland
- first_name: L. W. H. J.
full_name: Heling, L. W. H. J.
last_name: Heling
- first_name: A.
full_name: Mashaghi, A.
last_name: Mashaghi
- first_name: S. J.
full_name: Tans, S. J.
last_name: Tans
citation:
ama: 'Wruck F, Avellaneda Sarrió M, Naqvi MM, et al. Probing Single Chaperone Substrates.
In: Hiller S, Liu M, He L, eds. Biophysics of Molecular Chaperones. Vol
29. Royal Society of Chemistry; 2023:278-318. doi:10.1039/bk9781839165986-00278'
apa: Wruck, F., Avellaneda Sarrió, M., Naqvi, M. M., Koers, E. J., Till, K., Gross,
L., … Tans, S. J. (2023). Probing Single Chaperone Substrates. In S. Hiller, M.
Liu, & L. He (Eds.), Biophysics of Molecular Chaperones (Vol. 29, pp.
278–318). Royal Society of Chemistry. https://doi.org/10.1039/bk9781839165986-00278
chicago: Wruck, F., Mario Avellaneda Sarrió, M. M. Naqvi, E. J. Koers, K. Till,
L. Gross, F. Moayed, et al. “Probing Single Chaperone Substrates.” In Biophysics
of Molecular Chaperones, edited by Sebastian Hiller, Maili Liu, and Lichun
He, 29:278–318. Royal Society of Chemistry, 2023. https://doi.org/10.1039/bk9781839165986-00278.
ieee: F. Wruck et al., “Probing Single Chaperone Substrates,” in Biophysics
of Molecular Chaperones, vol. 29, S. Hiller, M. Liu, and L. He, Eds. Royal
Society of Chemistry, 2023, pp. 278–318.
ista: 'Wruck F, Avellaneda Sarrió M, Naqvi MM, Koers EJ, Till K, Gross L, Moayed
F, Roland A, Heling LWHJ, Mashaghi A, Tans SJ. 2023.Probing Single Chaperone Substrates.
In: Biophysics of Molecular Chaperones. New Developments in NMR, vol. 29, 278–318.'
mla: Wruck, F., et al. “Probing Single Chaperone Substrates.” Biophysics of Molecular
Chaperones, edited by Sebastian Hiller et al., vol. 29, Royal Society of Chemistry,
2023, pp. 278–318, doi:10.1039/bk9781839165986-00278.
short: F. Wruck, M. Avellaneda Sarrió, M.M. Naqvi, E.J. Koers, K. Till, L. Gross,
F. Moayed, A. Roland, L.W.H.J. Heling, A. Mashaghi, S.J. Tans, in:, S. Hiller,
M. Liu, L. He (Eds.), Biophysics of Molecular Chaperones, Royal Society of Chemistry,
2023, pp. 278–318.
date_created: 2024-01-22T08:07:02Z
date_published: 2023-11-01T00:00:00Z
date_updated: 2024-01-23T12:01:53Z
day: '01'
department:
- _id: MiSi
doi: 10.1039/bk9781839165986-00278
editor:
- first_name: Sebastian
full_name: Hiller, Sebastian
last_name: Hiller
- first_name: Maili
full_name: Liu, Maili
last_name: Liu
- first_name: Lichun
full_name: He, Lichun
last_name: He
intvolume: ' 29'
language:
- iso: eng
month: '11'
oa_version: None
page: 278-318
publication: Biophysics of Molecular Chaperones
publication_identifier:
eisbn:
- '9781839165993'
isbn:
- '9781839162824'
publication_status: published
publisher: Royal Society of Chemistry
quality_controlled: '1'
status: public
title: Probing Single Chaperone Substrates
type: book_chapter
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 29
year: '2023'
...