---
_id: '12114'
abstract:
- lang: eng
  text: 'Probing the dynamics of aromatic side chains provides important insights
    into the behavior of a protein because flips of aromatic rings in a protein’s
    hydrophobic core report on breathing motion involving a large part of the protein.
    Inherently invisible to crystallography, aromatic motions have been primarily
    studied by solution NMR. The question how packing of proteins in crystals affects
    ring flips has, thus, remained largely unexplored. Here we apply magic-angle spinning
    NMR, advanced phenylalanine 1H-13C/2H isotope labeling and MD simulation to a
    protein in three different crystal packing environments to shed light onto possible
    impact of packing on ring flips. The flips of the two Phe residues in ubiquitin,
    both surface exposed, appear remarkably conserved in the different crystal forms,
    even though the intermolecular packing is quite different: Phe4 flips on a ca.
    10–20 ns time scale, and Phe45 are broadened in all crystals, presumably due to
    µs motion. Our findings suggest that intramolecular influences are more important
    for ring flips than intermolecular (packing) effects.'
acknowledgement: The NMR platform in Grenoble is part of the Grenoble Instruct-ERIC
  center (ISBG; UAR 3518 CNRS-CEA-UGA-EMBL) within the Grenoble Partnership for Structural
  Biology (PSB), supported by FRISBI (ANR-10-INBS-0005-02) and GRAL, financed within
  the University Grenoble Alpes graduate school (Ecoles Universitaires de Recherche)
  CBH-EUR-GS (ANR-17-EURE-0003). This work was supported by the European Research
  Council (StG-2012-311318-ProtDyn2Function to P.S.) and used the platforms of the
  Grenoble Instruct Center (ISBG; UMS 3518 CNRS-CEA-UJF-EMBL) with support from FRISBI
  (ANR-10-INSB-05–02) and GRAL (ANR-10-LABX-49–01) within the Grenoble Partnership
  for Structural Biology (PSB). We would like to thank Sergei Izmailov for developing
  and maintaining the pyxmolpp2 library. N.R.S. acknowledges support from St. Petersburg
  State University in a form of the grant 92425251 and the access to the MRR, MCT
  and CAMR resource centers. P.S. thanks Malcolm Levitt for pointing out the fact
  that “tensor asymmetry” is better called “tensor biaxiality”.
article_number: '100079'
article_processing_charge: No
article_type: original
author:
- first_name: Diego F.
  full_name: Gauto, Diego F.
  last_name: Gauto
- first_name: Olga O.
  full_name: Lebedenko, Olga O.
  last_name: Lebedenko
- first_name: Lea Marie
  full_name: Becker, Lea Marie
  id: 36336939-eb97-11eb-a6c2-c83f1214ca79
  last_name: Becker
  orcid: 0000-0002-6401-5151
- first_name: Isabel
  full_name: Ayala, Isabel
  last_name: Ayala
- first_name: Roman
  full_name: Lichtenecker, Roman
  last_name: Lichtenecker
- first_name: Nikolai R.
  full_name: Skrynnikov, Nikolai R.
  last_name: Skrynnikov
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
citation:
  ama: 'Gauto DF, Lebedenko OO, Becker LM, et al. Aromatic ring flips in differently
    packed ubiquitin protein crystals from MAS NMR and MD. <i>Journal of Structural
    Biology: X</i>. 2023;7. doi:<a href="https://doi.org/10.1016/j.yjsbx.2022.100079">10.1016/j.yjsbx.2022.100079</a>'
  apa: 'Gauto, D. F., Lebedenko, O. O., Becker, L. M., Ayala, I., Lichtenecker, R.,
    Skrynnikov, N. R., &#38; Schanda, P. (2023). Aromatic ring flips in differently
    packed ubiquitin protein crystals from MAS NMR and MD. <i>Journal of Structural
    Biology: X</i>. Elsevier. <a href="https://doi.org/10.1016/j.yjsbx.2022.100079">https://doi.org/10.1016/j.yjsbx.2022.100079</a>'
  chicago: 'Gauto, Diego F., Olga O. Lebedenko, Lea Marie Becker, Isabel Ayala, Roman
    Lichtenecker, Nikolai R. Skrynnikov, and Paul Schanda. “Aromatic Ring Flips in
    Differently Packed Ubiquitin Protein Crystals from MAS NMR and MD.” <i>Journal
    of Structural Biology: X</i>. Elsevier, 2023. <a href="https://doi.org/10.1016/j.yjsbx.2022.100079">https://doi.org/10.1016/j.yjsbx.2022.100079</a>.'
  ieee: 'D. F. Gauto <i>et al.</i>, “Aromatic ring flips in differently packed ubiquitin
    protein crystals from MAS NMR and MD,” <i>Journal of Structural Biology: X</i>,
    vol. 7. Elsevier, 2023.'
  ista: 'Gauto DF, Lebedenko OO, Becker LM, Ayala I, Lichtenecker R, Skrynnikov NR,
    Schanda P. 2023. Aromatic ring flips in differently packed ubiquitin protein crystals
    from MAS NMR and MD. Journal of Structural Biology: X. 7, 100079.'
  mla: 'Gauto, Diego F., et al. “Aromatic Ring Flips in Differently Packed Ubiquitin
    Protein Crystals from MAS NMR and MD.” <i>Journal of Structural Biology: X</i>,
    vol. 7, 100079, Elsevier, 2023, doi:<a href="https://doi.org/10.1016/j.yjsbx.2022.100079">10.1016/j.yjsbx.2022.100079</a>.'
  short: 'D.F. Gauto, O.O. Lebedenko, L.M. Becker, I. Ayala, R. Lichtenecker, N.R.
    Skrynnikov, P. Schanda, Journal of Structural Biology: X 7 (2023).'
corr_author: '1'
date_created: 2023-01-12T11:55:38Z
date_published: 2023-01-01T00:00:00Z
date_updated: 2026-07-20T09:49:12Z
day: '01'
ddc:
- '570'
department:
- _id: PaSc
doi: 10.1016/j.yjsbx.2022.100079
external_id:
  pmid:
  - '36578472'
file:
- access_level: open_access
  checksum: b4b1c10a31018aafe053b7d55a470e54
  content_type: application/pdf
  creator: dernst
  date_created: 2023-08-16T09:36:28Z
  date_updated: 2023-08-16T09:36:28Z
  file_id: '14064'
  file_name: 2023_JourStrucBiologyX_Gauto.pdf
  file_size: 5132322
  relation: main_file
  success: 1
file_date_updated: 2023-08-16T09:36:28Z
fulldoi: https://doi.org/10.1016/j.yjsbx.2022.100079
has_accepted_license: '1'
intvolume: '         7'
keyword:
- Structural Biology
language:
- iso: eng
license: https://creativecommons.org/licenses/by-nc-nd/4.0/
month: '01'
oa: 1
oa_version: Published Version
pmid: 1
publication: 'Journal of Structural Biology: X'
publication_identifier:
  issn:
  - 2590-1524
publication_status: published
publisher: Elsevier
quality_controlled: '1'
related_material:
  record:
  - id: '22334'
    relation: dissertation_contains
    status: public
scopus_import: '1'
status: public
title: Aromatic ring flips in differently packed ubiquitin protein crystals from MAS
  NMR and MD
tmp:
  image: /images/cc_by_nc_nd.png
  legal_code_url: https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode
  name: Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International
    (CC BY-NC-ND 4.0)
  short: CC BY-NC-ND (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 7
year: '2023'
...
---
_id: '14036'
abstract:
- lang: eng
  text: Magic-angle spinning (MAS) nuclear magnetic resonance (NMR) is establishing
    itself as a powerful method for the characterization of protein dynamics at the
    atomic scale. We discuss here how R1ρ MAS relaxation dispersion NMR can explore
    microsecond-to-millisecond motions. Progress in instrumentation, isotope labeling,
    and pulse sequence design has paved the way for quantitative analyses of even
    rare structural fluctuations. In addition to isotropic chemical-shift fluctuations
    exploited in solution-state NMR relaxation dispersion experiments, MAS NMR has
    a wider arsenal of observables, allowing to see motions even if the exchanging
    states do not differ in their chemical shifts. We demonstrate the potential of
    the technique for probing motions in challenging large enzymes, membrane proteins,
    and protein assemblies.
acknowledgement: We thank Petra Rovó for critical reading of this manuscript. We acknowledge
  the Austrian Science Foundation FWF (project AlloSpace, number I5812–B) and funding
  by the Institute of Science and Technology Austria.
article_number: '102660'
article_processing_charge: Yes (via OA deal)
article_type: original
author:
- first_name: Federico
  full_name: Napoli, Federico
  id: d42e08e7-f4fc-11eb-af0a-d71e26138f1b
  last_name: Napoli
  orcid: 0000-0002-9043-136X
- first_name: Lea Marie
  full_name: Becker, Lea Marie
  id: 36336939-eb97-11eb-a6c2-c83f1214ca79
  last_name: Becker
  orcid: 0000-0002-6401-5151
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
citation:
  ama: Napoli F, Becker LM, Schanda P. Protein dynamics detected by magic-angle spinning
    relaxation dispersion NMR. <i>Current Opinion in Structural Biology</i>. 2023;82(10).
    doi:<a href="https://doi.org/10.1016/j.sbi.2023.102660">10.1016/j.sbi.2023.102660</a>
  apa: Napoli, F., Becker, L. M., &#38; Schanda, P. (2023). Protein dynamics detected
    by magic-angle spinning relaxation dispersion NMR. <i>Current Opinion in Structural
    Biology</i>. Elsevier. <a href="https://doi.org/10.1016/j.sbi.2023.102660">https://doi.org/10.1016/j.sbi.2023.102660</a>
  chicago: Napoli, Federico, Lea Marie Becker, and Paul Schanda. “Protein Dynamics
    Detected by Magic-Angle Spinning Relaxation Dispersion NMR.” <i>Current Opinion
    in Structural Biology</i>. Elsevier, 2023. <a href="https://doi.org/10.1016/j.sbi.2023.102660">https://doi.org/10.1016/j.sbi.2023.102660</a>.
  ieee: F. Napoli, L. M. Becker, and P. Schanda, “Protein dynamics detected by magic-angle
    spinning relaxation dispersion NMR,” <i>Current Opinion in Structural Biology</i>,
    vol. 82, no. 10. Elsevier, 2023.
  ista: Napoli F, Becker LM, Schanda P. 2023. Protein dynamics detected by magic-angle
    spinning relaxation dispersion NMR. Current Opinion in Structural Biology. 82(10),
    102660.
  mla: Napoli, Federico, et al. “Protein Dynamics Detected by Magic-Angle Spinning
    Relaxation Dispersion NMR.” <i>Current Opinion in Structural Biology</i>, vol.
    82, no. 10, 102660, Elsevier, 2023, doi:<a href="https://doi.org/10.1016/j.sbi.2023.102660">10.1016/j.sbi.2023.102660</a>.
  short: F. Napoli, L.M. Becker, P. Schanda, Current Opinion in Structural Biology
    82 (2023).
corr_author: '1'
date_created: 2023-08-13T22:01:11Z
date_published: 2023-10-01T00:00:00Z
date_updated: 2025-04-14T09:10:17Z
day: '01'
ddc:
- '570'
department:
- _id: PaSc
doi: 10.1016/j.sbi.2023.102660
external_id:
  isi:
  - '001053616200001'
  pmid:
  - '37536064'
file:
- access_level: open_access
  checksum: c850f7ac8a4234319755b672c1df69ae
  content_type: application/pdf
  creator: dernst
  date_created: 2024-01-30T12:36:39Z
  date_updated: 2024-01-30T12:36:39Z
  file_id: '14907'
  file_name: 2023_CurrentOpinionStrucBio_Napoli.pdf
  file_size: 1231998
  relation: main_file
  success: 1
file_date_updated: 2024-01-30T12:36:39Z
fulldoi: https://doi.org/10.1016/j.sbi.2023.102660
intvolume: '        82'
isi: 1
issue: '10'
language:
- iso: eng
license: https://creativecommons.org/licenses/by/4.0/
month: '10'
oa: 1
oa_version: Published Version
pmid: 1
project:
- _id: eb9c82eb-77a9-11ec-83b8-aadd536561cf
  grant_number: I05812
  name: AlloSpace. The emergence and mechanisms of allostery
publication: Current Opinion in Structural Biology
publication_identifier:
  eissn:
  - 1879-033X
  issn:
  - 0959-440X
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Protein dynamics detected by magic-angle spinning relaxation dispersion NMR
tmp:
  image: /images/cc_by.png
  legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
  name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
  short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 82
year: '2023'
...
---
_id: '11179'
abstract:
- lang: eng
  text: Large oligomeric enzymes control a myriad of cellular processes, from protein
    synthesis and degradation to metabolism. The 0.5 MDa large TET2 aminopeptidase,
    a prototypical protease important for cellular homeostasis, degrades peptides
    within a ca. 60 Å wide tetrahedral chamber with four lateral openings. The mechanisms
    of substrate trafficking and processing remain debated. Here, we integrate magic-angle
    spinning (MAS) NMR, mutagenesis, co-evolution analysis and molecular dynamics
    simulations and reveal that a loop in the catalytic chamber is a key element for
    enzymatic function. The loop is able to stabilize ligands in the active site and
    may additionally have a direct role in activating the catalytic water molecule
    whereby a conserved histidine plays a key role. Our data provide a strong case
    for the functional importance of highly dynamic - and often overlooked - parts
    of an enzyme, and the potential of MAS NMR to investigate their dynamics at atomic
    resolution.
acknowledgement: "We are grateful to Bernhard Brutscher, Alicia Vallet, and Adrien
  Favier for excellent NMR\r\nplatform operation and management. The plasmid coding
  for TET2 was kindly provided\r\nby Bruno Franzetti and Jerome Boisbouvier (IBS Grenoble).
  We thank Anne-Marie Villard\r\nand the RoBioMol platform for preparing the loop
  deletion construct. The RoBioMol\r\nplatform is part of the Grenoble Instruct-ERIC
  center (ISBG; UAR 3518 CNRS-CEAUGA-EMBL) within the Grenoble Partnership for Structural
  Biology (PSB), supported by FRISBI (ANR-10-INBS-0005-02) and GRAL (ANR-10-LABX-49-01),
  financed within the University Grenoble Alpes graduate school (Ecoles Universitaires
  de Recherche) CBHEUR-GS (ANR-17-EURE-0003). This work was supported by the European
  Research Council (StG-2012-311318-ProtDyn2Function to P. S.) and the French Agence
  Nationale de la Recherche (ANR), under grant ANR-14-ACHN-0016 (M.P. and A.B.)."
article_number: '1927'
article_processing_charge: No
article_type: original
author:
- first_name: Diego F.
  full_name: Gauto, Diego F.
  last_name: Gauto
- first_name: Pavel
  full_name: Macek, Pavel
  last_name: Macek
- first_name: Duccio
  full_name: Malinverni, Duccio
  last_name: Malinverni
- first_name: Hugo
  full_name: Fraga, Hugo
  last_name: Fraga
- first_name: Matteo
  full_name: Paloni, Matteo
  last_name: Paloni
- first_name: Iva
  full_name: Sučec, Iva
  last_name: Sučec
- first_name: Audrey
  full_name: Hessel, Audrey
  last_name: Hessel
- first_name: Juan Pablo
  full_name: Bustamante, Juan Pablo
  last_name: Bustamante
- first_name: Alessandro
  full_name: Barducci, Alessandro
  last_name: Barducci
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
citation:
  ama: Gauto DF, Macek P, Malinverni D, et al. Functional control of a 0.5 MDa TET
    aminopeptidase by a flexible loop revealed by MAS NMR. <i>Nature Communications</i>.
    2022;13. doi:<a href="https://doi.org/10.1038/s41467-022-29423-0">10.1038/s41467-022-29423-0</a>
  apa: Gauto, D. F., Macek, P., Malinverni, D., Fraga, H., Paloni, M., Sučec, I.,
    … Schanda, P. (2022). Functional control of a 0.5 MDa TET aminopeptidase by a
    flexible loop revealed by MAS NMR. <i>Nature Communications</i>. Springer Nature.
    <a href="https://doi.org/10.1038/s41467-022-29423-0">https://doi.org/10.1038/s41467-022-29423-0</a>
  chicago: Gauto, Diego F., Pavel Macek, Duccio Malinverni, Hugo Fraga, Matteo Paloni,
    Iva Sučec, Audrey Hessel, Juan Pablo Bustamante, Alessandro Barducci, and Paul
    Schanda. “Functional Control of a 0.5 MDa TET Aminopeptidase by a Flexible Loop
    Revealed by MAS NMR.” <i>Nature Communications</i>. Springer Nature, 2022. <a
    href="https://doi.org/10.1038/s41467-022-29423-0">https://doi.org/10.1038/s41467-022-29423-0</a>.
  ieee: D. F. Gauto <i>et al.</i>, “Functional control of a 0.5 MDa TET aminopeptidase
    by a flexible loop revealed by MAS NMR,” <i>Nature Communications</i>, vol. 13.
    Springer Nature, 2022.
  ista: Gauto DF, Macek P, Malinverni D, Fraga H, Paloni M, Sučec I, Hessel A, Bustamante
    JP, Barducci A, Schanda P. 2022. Functional control of a 0.5 MDa TET aminopeptidase
    by a flexible loop revealed by MAS NMR. Nature Communications. 13, 1927.
  mla: Gauto, Diego F., et al. “Functional Control of a 0.5 MDa TET Aminopeptidase
    by a Flexible Loop Revealed by MAS NMR.” <i>Nature Communications</i>, vol. 13,
    1927, Springer Nature, 2022, doi:<a href="https://doi.org/10.1038/s41467-022-29423-0">10.1038/s41467-022-29423-0</a>.
  short: D.F. Gauto, P. Macek, D. Malinverni, H. Fraga, M. Paloni, I. Sučec, A. Hessel,
    J.P. Bustamante, A. Barducci, P. Schanda, Nature Communications 13 (2022).
corr_author: '1'
date_created: 2022-04-17T22:01:45Z
date_published: 2022-04-08T00:00:00Z
date_updated: 2025-06-11T13:31:55Z
day: '08'
ddc:
- '570'
department:
- _id: PaSc
doi: 10.1038/s41467-022-29423-0
external_id:
  isi:
  - '000781498700009'
  pmid:
  - '35395851'
file:
- access_level: open_access
  checksum: db61d5534e988743d6266d3675d77b08
  content_type: application/pdf
  creator: dernst
  date_created: 2022-05-02T08:48:00Z
  date_updated: 2022-05-02T08:48:00Z
  file_id: '11348'
  file_name: 2022_NatureCommunications_Gauto.pdf
  file_size: 2637590
  relation: main_file
  success: 1
file_date_updated: 2022-05-02T08:48:00Z
fulldoi: https://doi.org/10.1038/s41467-022-29423-0
has_accepted_license: '1'
intvolume: '        13'
isi: 1
language:
- iso: eng
month: '04'
oa: 1
oa_version: Published Version
pmid: 1
publication: Nature Communications
publication_identifier:
  eissn:
  - 2041-1723
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
related_material:
  link:
  - relation: erratum
    url: https://doi.org/10.1038/s41467-022-31243-1
scopus_import: '1'
status: public
title: Functional control of a 0.5 MDa TET aminopeptidase by a flexible loop revealed
  by MAS NMR
tmp:
  image: /images/cc_by.png
  legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
  name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
  short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 13
year: '2022'
...
---
_id: '10323'
abstract:
- lang: eng
  text: Molecular chaperones are central to cellular protein homeostasis. Dynamic
    disorder is a key feature of the complexes of molecular chaperones and their client
    proteins, and it facilitates the client release towards a folded state or the
    handover to downstream components. The dynamic nature also implies that a given
    chaperone can interact with many different client proteins, based on physico-chemical
    sequence properties rather than on structural complementarity of their (folded)
    3D structure. Yet, the balance between this promiscuity and some degree of client
    specificity is poorly understood. Here, we review recent atomic-level descriptions
    of chaperones with client proteins, including chaperones in complex with intrinsically
    disordered proteins, with membrane-protein precursors, or partially folded client
    proteins. We focus hereby on chaperone-client interactions that are independent
    of ATP. The picture emerging from these studies highlights the importance of dynamics
    in these complexes, whereby several interaction types, not only hydrophobic ones,
    contribute to the complex formation. We discuss these features of chaperone-client
    complexes and possible factors that may contribute to this balance of promiscuity
    and specificity.
acknowledgement: We thank Juan C. Fontecilla-Camps for insightful discussions related
  to ATP-driven machineries, and Elif Karagöz for providing the structural model of
  the Hsp90-Tau complex. This study was supported by the European Research Council
  (StG-2012-311318-ProtDyn2Function) and the Agence Nationale de la Recherche (ANR-18-CE92-0032-MitoMemProtImp).
article_number: '762005'
article_processing_charge: Yes (via OA deal)
article_type: original
author:
- first_name: Iva
  full_name: Sučec, Iva
  last_name: Sučec
- first_name: Beate
  full_name: Bersch, Beate
  last_name: Bersch
- 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, Bersch B, Schanda P. How do chaperones bind (partly) unfolded client
    proteins? <i>Frontiers in Molecular Biosciences</i>. 2021;8. doi:<a href="https://doi.org/10.3389/fmolb.2021.762005">10.3389/fmolb.2021.762005</a>
  apa: Sučec, I., Bersch, B., &#38; Schanda, P. (2021). How do chaperones bind (partly)
    unfolded client proteins? <i>Frontiers in Molecular Biosciences</i>. Frontiers.
    <a href="https://doi.org/10.3389/fmolb.2021.762005">https://doi.org/10.3389/fmolb.2021.762005</a>
  chicago: Sučec, Iva, Beate Bersch, and Paul Schanda. “How Do Chaperones Bind (Partly)
    Unfolded Client Proteins?” <i>Frontiers in Molecular Biosciences</i>. Frontiers,
    2021. <a href="https://doi.org/10.3389/fmolb.2021.762005">https://doi.org/10.3389/fmolb.2021.762005</a>.
  ieee: I. Sučec, B. Bersch, and P. Schanda, “How do chaperones bind (partly) unfolded
    client proteins?,” <i>Frontiers in Molecular Biosciences</i>, vol. 8. Frontiers,
    2021.
  ista: Sučec I, Bersch B, Schanda P. 2021. How do chaperones bind (partly) unfolded
    client proteins? Frontiers in Molecular Biosciences. 8, 762005.
  mla: Sučec, Iva, et al. “How Do Chaperones Bind (Partly) Unfolded Client Proteins?”
    <i>Frontiers in Molecular Biosciences</i>, vol. 8, 762005, Frontiers, 2021, doi:<a
    href="https://doi.org/10.3389/fmolb.2021.762005">10.3389/fmolb.2021.762005</a>.
  short: I. Sučec, B. Bersch, P. Schanda, Frontiers in Molecular Biosciences 8 (2021).
corr_author: '1'
date_created: 2021-11-21T23:01:29Z
date_published: 2021-10-25T00:00:00Z
date_updated: 2024-10-09T21:01:12Z
day: '25'
ddc:
- '547'
department:
- _id: PaSc
doi: 10.3389/fmolb.2021.762005
external_id:
  isi:
  - '000717241700001'
  pmid:
  - '34760928'
file:
- access_level: open_access
  checksum: a5c9dbf80dc2c5aaa737f456c941d964
  content_type: application/pdf
  creator: cchlebak
  date_created: 2021-11-23T15:06:58Z
  date_updated: 2021-11-23T15:06:58Z
  file_id: '10333'
  file_name: 2021_FrontiersMolBioSc_Sučec.pdf
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publication: Frontiers in Molecular Biosciences
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title: How do chaperones bind (partly) unfolded client proteins?
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