---
_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).
date_created: 2023-08-13T22:01:11Z
date_published: 2023-10-01T00:00:00Z
date_updated: 2024-01-30T12:37:36Z
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
intvolume: '        82'
isi: 1
issue: '10'
language:
- iso: eng
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: '11167'
abstract:
- lang: eng
  text: Complex I is one of the major respiratory complexes, conserved from bacteria
    to mammals. It oxidises NADH, reduces quinone and pumps protons across the membrane,
    thus playing a central role in the oxidative energy metabolism. In this review
    we discuss our current state of understanding the structure of complex I from
    various species of mammals, plants, fungi, and bacteria, as well as of several
    complex I-related proteins. By comparing the structural evidence from these systems
    in different redox states and data from mutagenesis and molecular simulations,
    we formulate the mechanisms of electron transfer and proton pumping and explain
    how they are conformationally and electrostatically coupled. Finally, we discuss
    the structural basis of the deactivation phenomenon in mammalian complex I.
article_number: '102350'
article_processing_charge: Yes (via OA deal)
article_type: original
author:
- first_name: Domen
  full_name: Kampjut, Domen
  id: 37233050-F248-11E8-B48F-1D18A9856A87
  last_name: Kampjut
- first_name: Leonid A
  full_name: Sazanov, Leonid A
  id: 338D39FE-F248-11E8-B48F-1D18A9856A87
  last_name: Sazanov
  orcid: 0000-0002-0977-7989
citation:
  ama: Kampjut D, Sazanov LA. Structure of respiratory complex I – An emerging blueprint
    for the mechanism. <i>Current Opinion in Structural Biology</i>. 2022;74. doi:<a
    href="https://doi.org/10.1016/j.sbi.2022.102350">10.1016/j.sbi.2022.102350</a>
  apa: Kampjut, D., &#38; Sazanov, L. A. (2022). Structure of respiratory complex
    I – An emerging blueprint for the mechanism. <i>Current Opinion in Structural
    Biology</i>. Elsevier. <a href="https://doi.org/10.1016/j.sbi.2022.102350">https://doi.org/10.1016/j.sbi.2022.102350</a>
  chicago: Kampjut, Domen, and Leonid A Sazanov. “Structure of Respiratory Complex
    I – An Emerging Blueprint for the Mechanism.” <i>Current Opinion in Structural
    Biology</i>. Elsevier, 2022. <a href="https://doi.org/10.1016/j.sbi.2022.102350">https://doi.org/10.1016/j.sbi.2022.102350</a>.
  ieee: D. Kampjut and L. A. Sazanov, “Structure of respiratory complex I – An emerging
    blueprint for the mechanism,” <i>Current Opinion in Structural Biology</i>, vol.
    74. Elsevier, 2022.
  ista: Kampjut D, Sazanov LA. 2022. Structure of respiratory complex I – An emerging
    blueprint for the mechanism. Current Opinion in Structural Biology. 74, 102350.
  mla: Kampjut, Domen, and Leonid A. Sazanov. “Structure of Respiratory Complex I
    – An Emerging Blueprint for the Mechanism.” <i>Current Opinion in Structural Biology</i>,
    vol. 74, 102350, Elsevier, 2022, doi:<a href="https://doi.org/10.1016/j.sbi.2022.102350">10.1016/j.sbi.2022.102350</a>.
  short: D. Kampjut, L.A. Sazanov, Current Opinion in Structural Biology 74 (2022).
date_created: 2022-04-15T09:32:35Z
date_published: 2022-06-01T00:00:00Z
date_updated: 2023-08-03T06:31:06Z
day: '01'
ddc:
- '570'
department:
- _id: LeSa
doi: 10.1016/j.sbi.2022.102350
external_id:
  isi:
  - '000829029500020'
  pmid:
  - '35316665'
file:
- access_level: open_access
  checksum: 72bdde48853643a32d42b75f54965c44
  content_type: application/pdf
  creator: dernst
  date_created: 2022-08-05T05:56:03Z
  date_updated: 2022-08-05T05:56:03Z
  file_id: '11725'
  file_name: 2022_CurrentOpStructBiology_Kampjut.pdf
  file_size: 815607
  relation: main_file
  success: 1
file_date_updated: 2022-08-05T05:56:03Z
has_accepted_license: '1'
intvolume: '        74'
isi: 1
keyword:
- Molecular Biology
- Structural Biology
language:
- iso: eng
month: '06'
oa: 1
oa_version: Published Version
pmid: 1
publication: Current Opinion in Structural Biology
publication_identifier:
  issn:
  - 0959-440X
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Structure of respiratory complex I – An emerging blueprint for the mechanism
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: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 74
year: '2022'
...
---
_id: '6343'
abstract:
- lang: eng
  text: Cryo-electron tomography (cryo-ET) provides unprecedented insights into the
    molecular constituents of biological environments. In combination with an image
    processing method called subtomogram averaging (STA), detailed 3D structures of
    biological molecules can be obtained in large, irregular macromolecular assemblies
    or in situ, without the need for purification. The contextual meta-information
    these methods also provide, such as a protein’s location within its native environment,
    can then be combined with functional data. This allows the derivation of a detailed
    view on the physiological or pathological roles of proteins from the molecular
    to cellular level. Despite their tremendous potential in in situ structural biology,
    cryo-ET and STA have been restricted by methodological limitations, such as the
    low obtainable resolution. Exciting progress now allows one to reach unprecedented
    resolutions in situ, ranging in optimal cases beyond the nanometer barrier. Here,
    I review current frontiers and future challenges in routinely determining high-resolution
    structures in in situ environments using cryo-ET and STA.
acknowledgement: The author acknowledges support from IST Austria and the Austrian
  Science Fund (FWF).
article_processing_charge: No
article_type: original
author:
- first_name: Florian KM
  full_name: Schur, Florian KM
  id: 48AD8942-F248-11E8-B48F-1D18A9856A87
  last_name: Schur
  orcid: 0000-0003-4790-8078
citation:
  ama: Schur FK. Toward high-resolution in situ structural biology with cryo-electron
    tomography and subtomogram averaging. <i>Current Opinion in Structural Biology</i>.
    2019;58(10):1-9. doi:<a href="https://doi.org/10.1016/j.sbi.2019.03.018">10.1016/j.sbi.2019.03.018</a>
  apa: Schur, F. K. (2019). Toward high-resolution in situ structural biology with
    cryo-electron tomography and subtomogram averaging. <i>Current Opinion in Structural
    Biology</i>. Elsevier. <a href="https://doi.org/10.1016/j.sbi.2019.03.018">https://doi.org/10.1016/j.sbi.2019.03.018</a>
  chicago: Schur, Florian KM. “Toward High-Resolution in Situ Structural Biology with
    Cryo-Electron Tomography and Subtomogram Averaging.” <i>Current Opinion in Structural
    Biology</i>. Elsevier, 2019. <a href="https://doi.org/10.1016/j.sbi.2019.03.018">https://doi.org/10.1016/j.sbi.2019.03.018</a>.
  ieee: F. K. Schur, “Toward high-resolution in situ structural biology with cryo-electron
    tomography and subtomogram averaging,” <i>Current Opinion in Structural Biology</i>,
    vol. 58, no. 10. Elsevier, pp. 1–9, 2019.
  ista: Schur FK. 2019. Toward high-resolution in situ structural biology with cryo-electron
    tomography and subtomogram averaging. Current Opinion in Structural Biology. 58(10),
    1–9.
  mla: Schur, Florian KM. “Toward High-Resolution in Situ Structural Biology with
    Cryo-Electron Tomography and Subtomogram Averaging.” <i>Current Opinion in Structural
    Biology</i>, vol. 58, no. 10, Elsevier, 2019, pp. 1–9, doi:<a href="https://doi.org/10.1016/j.sbi.2019.03.018">10.1016/j.sbi.2019.03.018</a>.
  short: F.K. Schur, Current Opinion in Structural Biology 58 (2019) 1–9.
date_created: 2019-04-19T11:19:13Z
date_published: 2019-10-01T00:00:00Z
date_updated: 2023-08-25T10:13:31Z
day: '01'
department:
- _id: FlSc
doi: 10.1016/j.sbi.2019.03.018
external_id:
  isi:
  - '000494891800004'
intvolume: '        58'
isi: 1
issue: '10'
language:
- iso: eng
month: '10'
oa_version: None
page: 1-9
publication: Current Opinion in Structural Biology
publication_identifier:
  issn:
  - 0959-440X
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Toward high-resolution in situ structural biology with cryo-electron tomography
  and subtomogram averaging
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 58
year: '2019'
...
---
_id: '10355'
abstract:
- lang: eng
  text: The molecular machinery of life is largely created via self-organisation of
    individual molecules into functional assemblies. Minimal coarse-grained models,
    in which a whole macromolecule is represented by a small number of particles,
    can be of great value in identifying the main driving forces behind self-organisation
    in cell biology. Such models can incorporate data from both molecular and continuum
    scales, and their results can be directly compared to experiments. Here we review
    the state of the art of models for studying the formation and biological function
    of macromolecular assemblies in living organisms. We outline the key ingredients
    of each model and their main findings. We illustrate the contribution of this
    class of simulations to identifying the physical mechanisms behind life and diseases,
    and discuss their future developments.
acknowledgement: We acknowledge funding from EPSRC (A.E.H. and A.Š.), the Academy
  of Medical Sciences (J.K. and A.Š.), the Wellcome Trust (J.K. and A.Š.), and the
  Royal Society (A.Š.). We thank Shiladitya Banerjee and Nikola Ojkic for critically
  reading the manuscript, and Claudia Flandoli for helping us with figures and illustrations.
article_processing_charge: No
article_type: original
author:
- first_name: Anne E
  full_name: Hafner, Anne E
  last_name: Hafner
- first_name: Johannes
  full_name: Krausser, Johannes
  last_name: Krausser
- first_name: Anđela
  full_name: Šarić, Anđela
  id: bf63d406-f056-11eb-b41d-f263a6566d8b
  last_name: Šarić
  orcid: 0000-0002-7854-2139
citation:
  ama: Hafner AE, Krausser J, Šarić A. Minimal coarse-grained models for molecular
    self-organisation in biology. <i>Current Opinion in Structural Biology</i>. 2019;58:43-52.
    doi:<a href="https://doi.org/10.1016/j.sbi.2019.05.018">10.1016/j.sbi.2019.05.018</a>
  apa: Hafner, A. E., Krausser, J., &#38; Šarić, A. (2019). Minimal coarse-grained
    models for molecular self-organisation in biology. <i>Current Opinion in Structural
    Biology</i>. Elsevier. <a href="https://doi.org/10.1016/j.sbi.2019.05.018">https://doi.org/10.1016/j.sbi.2019.05.018</a>
  chicago: Hafner, Anne E, Johannes Krausser, and Anđela Šarić. “Minimal Coarse-Grained
    Models for Molecular Self-Organisation in Biology.” <i>Current Opinion in Structural
    Biology</i>. Elsevier, 2019. <a href="https://doi.org/10.1016/j.sbi.2019.05.018">https://doi.org/10.1016/j.sbi.2019.05.018</a>.
  ieee: A. E. Hafner, J. Krausser, and A. Šarić, “Minimal coarse-grained models for
    molecular self-organisation in biology,” <i>Current Opinion in Structural Biology</i>,
    vol. 58. Elsevier, pp. 43–52, 2019.
  ista: Hafner AE, Krausser J, Šarić A. 2019. Minimal coarse-grained models for molecular
    self-organisation in biology. Current Opinion in Structural Biology. 58, 43–52.
  mla: Hafner, Anne E., et al. “Minimal Coarse-Grained Models for Molecular Self-Organisation
    in Biology.” <i>Current Opinion in Structural Biology</i>, vol. 58, Elsevier,
    2019, pp. 43–52, doi:<a href="https://doi.org/10.1016/j.sbi.2019.05.018">10.1016/j.sbi.2019.05.018</a>.
  short: A.E. Hafner, J. Krausser, A. Šarić, Current Opinion in Structural Biology
    58 (2019) 43–52.
date_created: 2021-11-26T11:33:21Z
date_published: 2019-06-18T00:00:00Z
date_updated: 2021-11-26T11:54:25Z
day: '18'
doi: 10.1016/j.sbi.2019.05.018
extern: '1'
external_id:
  pmid:
  - '31226513'
intvolume: '        58'
keyword:
- molecular biology
- structural biology
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://arxiv.org/abs/1906.09349
month: '06'
oa: 1
oa_version: Preprint
page: 43-52
pmid: 1
publication: Current Opinion in Structural Biology
publication_identifier:
  issn:
  - 0959-440X
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Minimal coarse-grained models for molecular self-organisation in biology
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 58
year: '2019'
...