---
_id: '10622'
abstract:
- lang: eng
text: We demonstrate a method for manipulating small ensembles of vortices in multiply
connected superconducting structures. A micron-size magnetic particle attached
to the tip of a silicon cantilever is used to locally apply magnetic flux through
the superconducting structure. By scanning the tip over the surface of the device
and by utilizing the dynamical coupling between the vortices and the cantilever,
a high-resolution spatial map of the different vortex configurations is obtained.
Moving the tip to a particular location in the map stabilizes a distinct multivortex
configuration. Thus, the scanning of the tip over a particular trajectory in space
permits nontrivial operations to be performed, such as braiding of individual
vortices within a larger vortex ensemble—a key capability required by many proposals
for topological quantum computing.
acknowledgement: We are grateful to Nadya Mason, Taylor Hughes, and Alexey Bezryadin
for useful discussions. This work was supported by the DOE Basic Energy Sciences
under DE-SC0012649 and the Department of Physics and the Frederick Seitz Materials
Research Laboratory Central Facilities at the University of Illinois.
article_processing_charge: No
article_type: original
arxiv: 1
author:
- first_name: Hryhoriy
full_name: Polshyn, Hryhoriy
id: edfc7cb1-526e-11ec-b05a-e6ecc27e4e48
last_name: Polshyn
orcid: 0000-0001-8223-8896
- first_name: Tyler
full_name: Naibert, Tyler
last_name: Naibert
- first_name: Raffi
full_name: Budakian, Raffi
last_name: Budakian
citation:
ama: Polshyn H, Naibert T, Budakian R. Manipulating multivortex states in superconducting
structures. Nano Letters. 2019;19(8):5476-5482. doi:10.1021/acs.nanolett.9b01983
apa: Polshyn, H., Naibert, T., & Budakian, R. (2019). Manipulating multivortex
states in superconducting structures. Nano Letters. American Chemical Society.
https://doi.org/10.1021/acs.nanolett.9b01983
chicago: Polshyn, Hryhoriy, Tyler Naibert, and Raffi Budakian. “Manipulating Multivortex
States in Superconducting Structures.” Nano Letters. American Chemical
Society, 2019. https://doi.org/10.1021/acs.nanolett.9b01983.
ieee: H. Polshyn, T. Naibert, and R. Budakian, “Manipulating multivortex states
in superconducting structures,” Nano Letters, vol. 19, no. 8. American
Chemical Society, pp. 5476–5482, 2019.
ista: Polshyn H, Naibert T, Budakian R. 2019. Manipulating multivortex states in
superconducting structures. Nano Letters. 19(8), 5476–5482.
mla: Polshyn, Hryhoriy, et al. “Manipulating Multivortex States in Superconducting
Structures.” Nano Letters, vol. 19, no. 8, American Chemical Society, 2019,
pp. 5476–82, doi:10.1021/acs.nanolett.9b01983.
short: H. Polshyn, T. Naibert, R. Budakian, Nano Letters 19 (2019) 5476–5482.
date_created: 2022-01-13T15:11:14Z
date_published: 2019-06-27T00:00:00Z
date_updated: 2022-01-13T15:41:24Z
day: '27'
doi: 10.1021/acs.nanolett.9b01983
extern: '1'
external_id:
arxiv:
- '1905.06303'
pmid:
- '31246034'
intvolume: ' 19'
issue: '8'
keyword:
- mechanical engineering
- condensed matter physics
- general materials science
- general chemistry
- bioengineering
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://arxiv.org/abs/1905.06303
month: '06'
oa: 1
oa_version: Preprint
page: 5476-5482
pmid: 1
publication: Nano Letters
publication_identifier:
eissn:
- 1530-6992
issn:
- 1530-6984
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Manipulating multivortex states in superconducting structures
type: journal_article
user_id: ea97e931-d5af-11eb-85d4-e6957dddbf17
volume: 19
year: '2019'
...
---
_id: '8405'
abstract:
- lang: eng
text: Atomic-resolution structure determination is crucial for understanding protein
function. Cryo-EM and NMR spectroscopy both provide structural information, but
currently cryo-EM does not routinely give access to atomic-level structural data,
and, generally, NMR structure determination is restricted to small (<30 kDa) proteins.
We introduce an integrated structure determination approach that simultaneously
uses NMR and EM data to overcome the limits of each of these methods. The approach
enables structure determination of the 468 kDa large dodecameric aminopeptidase
TET2 to a precision and accuracy below 1 Å by combining secondary-structure information
obtained from near-complete magic-angle-spinning NMR assignments of the 39 kDa-large
subunits, distance restraints from backbone amides and ILV methyl groups, and
a 4.1 Å resolution EM map. The resulting structure exceeds current standards of
NMR and EM structure determination in terms of molecular weight and precision.
Importantly, the approach is successful even in cases where only medium-resolution
cryo-EM data are available.
article_number: '2697'
article_processing_charge: No
article_type: original
author:
- first_name: Diego F.
full_name: Gauto, Diego F.
last_name: Gauto
- first_name: Leandro F.
full_name: Estrozi, Leandro F.
last_name: Estrozi
- first_name: Charles D.
full_name: Schwieters, Charles D.
last_name: Schwieters
- first_name: Gregory
full_name: Effantin, Gregory
last_name: Effantin
- first_name: Pavel
full_name: Macek, Pavel
last_name: Macek
- first_name: Remy
full_name: Sounier, Remy
last_name: Sounier
- first_name: Astrid C.
full_name: Sivertsen, Astrid C.
last_name: Sivertsen
- first_name: Elena
full_name: Schmidt, Elena
last_name: Schmidt
- first_name: Rime
full_name: Kerfah, Rime
last_name: Kerfah
- first_name: Guillaume
full_name: Mas, Guillaume
last_name: Mas
- first_name: Jacques-Philippe
full_name: Colletier, Jacques-Philippe
last_name: Colletier
- first_name: Peter
full_name: Güntert, Peter
last_name: Güntert
- first_name: Adrien
full_name: Favier, Adrien
last_name: Favier
- first_name: Guy
full_name: Schoehn, Guy
last_name: Schoehn
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Jerome
full_name: Boisbouvier, Jerome
last_name: Boisbouvier
citation:
ama: Gauto DF, Estrozi LF, Schwieters CD, et al. Integrated NMR and cryo-EM atomic-resolution
structure determination of a half-megadalton enzyme complex. Nature Communications.
2019;10. doi:10.1038/s41467-019-10490-9
apa: Gauto, D. F., Estrozi, L. F., Schwieters, C. D., Effantin, G., Macek, P., Sounier,
R., … Boisbouvier, J. (2019). Integrated NMR and cryo-EM atomic-resolution structure
determination of a half-megadalton enzyme complex. Nature Communications.
Springer Nature. https://doi.org/10.1038/s41467-019-10490-9
chicago: Gauto, Diego F., Leandro F. Estrozi, Charles D. Schwieters, Gregory Effantin,
Pavel Macek, Remy Sounier, Astrid C. Sivertsen, et al. “Integrated NMR and Cryo-EM
Atomic-Resolution Structure Determination of a Half-Megadalton Enzyme Complex.”
Nature Communications. Springer Nature, 2019. https://doi.org/10.1038/s41467-019-10490-9.
ieee: D. F. Gauto et al., “Integrated NMR and cryo-EM atomic-resolution structure
determination of a half-megadalton enzyme complex,” Nature Communications,
vol. 10. Springer Nature, 2019.
ista: Gauto DF, Estrozi LF, Schwieters CD, Effantin G, Macek P, Sounier R, Sivertsen
AC, Schmidt E, Kerfah R, Mas G, Colletier J-P, Güntert P, Favier A, Schoehn G,
Schanda P, Boisbouvier J. 2019. Integrated NMR and cryo-EM atomic-resolution structure
determination of a half-megadalton enzyme complex. Nature Communications. 10,
2697.
mla: Gauto, Diego F., et al. “Integrated NMR and Cryo-EM Atomic-Resolution Structure
Determination of a Half-Megadalton Enzyme Complex.” Nature Communications,
vol. 10, 2697, Springer Nature, 2019, doi:10.1038/s41467-019-10490-9.
short: D.F. Gauto, L.F. Estrozi, C.D. Schwieters, G. Effantin, P. Macek, R. Sounier,
A.C. Sivertsen, E. Schmidt, R. Kerfah, G. Mas, J.-P. Colletier, P. Güntert, A.
Favier, G. Schoehn, P. Schanda, J. Boisbouvier, Nature Communications 10 (2019).
date_created: 2020-09-17T10:28:25Z
date_published: 2019-06-19T00:00:00Z
date_updated: 2021-01-12T08:19:03Z
day: '19'
doi: 10.1038/s41467-019-10490-9
extern: '1'
external_id:
pmid:
- '31217444'
intvolume: ' 10'
keyword:
- General Biochemistry
- Genetics and Molecular Biology
- General Physics and Astronomy
- General Chemistry
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1038/s41467-019-10490-9
month: '06'
oa: 1
oa_version: Published Version
pmid: 1
publication: Nature Communications
publication_identifier:
issn:
- 2041-1723
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton
enzyme complex
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 10
year: '2019'
...
---
_id: '8408'
abstract:
- lang: eng
text: Aromatic residues are located at structurally important sites of many proteins.
Probing their interactions and dynamics can provide important functional insight
but is challenging in large proteins. Here, we introduce approaches to characterize
dynamics of phenylalanine residues using 1H-detected fast magic-angle spinning
(MAS) NMR combined with a tailored isotope-labeling scheme. Our approach yields
isolated two-spin systems that are ideally suited for artefact-free dynamics measurements,
and allows probing motions effectively without molecular-weight limitations. The
application to the TET2 enzyme assembly of ~0.5 MDa size, the currently largest
protein assigned by MAS NMR, provides insights into motions occurring on a wide
range of time scales (ps-ms). We quantitatively probe ring flip motions, and show
the temperature dependence by MAS NMR measurements down to 100 K. Interestingly,
favorable line widths are observed down to 100 K, with potential implications
for DNP NMR. Furthermore, we report the first 13C R1ρ MAS NMR relaxation-dispersion
measurements and detect structural excursions occurring on a microsecond time
scale in the entry pore to the catalytic chamber and at a trimer interface that
was proposed as exit pore. We show that the labeling scheme with deuteration at
ca. 50 kHz MAS provides superior resolution compared to 100 kHz MAS experiments
with protonated, uniformly 13C-labeled samples.
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: Alessandro
full_name: Barducci, Alessandro
last_name: Barducci
- first_name: Hugo
full_name: Fraga, Hugo
last_name: Fraga
- first_name: Audrey
full_name: Hessel, Audrey
last_name: Hessel
- first_name: Tsutomu
full_name: Terauchi, Tsutomu
last_name: Terauchi
- first_name: David
full_name: Gajan, David
last_name: Gajan
- first_name: Yohei
full_name: Miyanoiri, Yohei
last_name: Miyanoiri
- first_name: Jerome
full_name: Boisbouvier, Jerome
last_name: Boisbouvier
- first_name: Roman
full_name: Lichtenecker, Roman
last_name: Lichtenecker
- first_name: Masatsune
full_name: Kainosho, Masatsune
last_name: Kainosho
- 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, Barducci A, et al. Aromatic ring dynamics, thermal activation,
and transient conformations of a 468 kDa enzyme by specific 1H–13C labeling and
fast magic-angle spinning NMR. Journal of the American Chemical Society.
2019;141(28):11183-11195. doi:10.1021/jacs.9b04219
apa: Gauto, D. F., Macek, P., Barducci, A., Fraga, H., Hessel, A., Terauchi, T.,
… Schanda, P. (2019). Aromatic ring dynamics, thermal activation, and transient
conformations of a 468 kDa enzyme by specific 1H–13C labeling and fast magic-angle
spinning NMR. Journal of the American Chemical Society. American Chemical
Society. https://doi.org/10.1021/jacs.9b04219
chicago: Gauto, Diego F., Pavel Macek, Alessandro Barducci, Hugo Fraga, Audrey Hessel,
Tsutomu Terauchi, David Gajan, et al. “Aromatic Ring Dynamics, Thermal Activation,
and Transient Conformations of a 468 KDa Enzyme by Specific 1H–13C Labeling and
Fast Magic-Angle Spinning NMR.” Journal of the American Chemical Society.
American Chemical Society, 2019. https://doi.org/10.1021/jacs.9b04219.
ieee: D. F. Gauto et al., “Aromatic ring dynamics, thermal activation, and
transient conformations of a 468 kDa enzyme by specific 1H–13C labeling and fast
magic-angle spinning NMR,” Journal of the American Chemical Society, vol.
141, no. 28. American Chemical Society, pp. 11183–11195, 2019.
ista: Gauto DF, Macek P, Barducci A, Fraga H, Hessel A, Terauchi T, Gajan D, Miyanoiri
Y, Boisbouvier J, Lichtenecker R, Kainosho M, Schanda P. 2019. Aromatic ring dynamics,
thermal activation, and transient conformations of a 468 kDa enzyme by specific
1H–13C labeling and fast magic-angle spinning NMR. Journal of the American Chemical
Society. 141(28), 11183–11195.
mla: Gauto, Diego F., et al. “Aromatic Ring Dynamics, Thermal Activation, and Transient
Conformations of a 468 KDa Enzyme by Specific 1H–13C Labeling and Fast Magic-Angle
Spinning NMR.” Journal of the American Chemical Society, vol. 141, no.
28, American Chemical Society, 2019, pp. 11183–95, doi:10.1021/jacs.9b04219.
short: D.F. Gauto, P. Macek, A. Barducci, H. Fraga, A. Hessel, T. Terauchi, D. Gajan,
Y. Miyanoiri, J. Boisbouvier, R. Lichtenecker, M. Kainosho, P. Schanda, Journal
of the American Chemical Society 141 (2019) 11183–11195.
date_created: 2020-09-17T10:29:00Z
date_published: 2019-06-14T00:00:00Z
date_updated: 2021-01-12T08:19:04Z
day: '14'
doi: 10.1021/jacs.9b04219
extern: '1'
external_id:
pmid:
- '31199882'
intvolume: ' 141'
issue: '28'
keyword:
- Colloid and Surface Chemistry
- Biochemistry
- General Chemistry
- Catalysis
language:
- iso: eng
month: '06'
oa_version: Submitted Version
page: 11183-11195
pmid: 1
publication: Journal of the American Chemical Society
publication_identifier:
issn:
- 0002-7863
- 1520-5126
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
status: public
title: Aromatic ring dynamics, thermal activation, and transient conformations of
a 468 kDa enzyme by specific 1H–13C labeling and fast magic-angle spinning NMR
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 141
year: '2019'
...
---
_id: '8413'
abstract:
- lang: eng
text: NMR relaxation dispersion methods provide a holistic way to observe microsecond
time-scale protein backbone motion both in solution and in the solid state. Different
nuclei (1H and 15N) and different relaxation dispersion techniques (Bloch–McConnell
and near-rotary-resonance) give complementary information about the amplitudes
and time scales of the conformational dynamics and provide comprehensive insights
into the mechanistic details of the structural rearrangements. In this paper,
we exemplify the benefits of the combination of various solution- and solid-state
relaxation dispersion methods on a microcrystalline protein (α-spectrin SH3 domain),
for which we are able to identify and model the functionally relevant conformational
rearrangements around the ligand recognition loop occurring on multiple microsecond
time scales. The observed loop motions suggest that the SH3 domain exists in a
binding-competent conformation in dynamic equilibrium with a sterically impaired
ground-state conformation both in solution and in crystalline form. This inherent
plasticity between the interconverting macrostates is compatible with a conformational-preselection
model and provides new insights into the recognition mechanisms of SH3 domains.
article_processing_charge: No
article_type: original
author:
- first_name: Petra
full_name: Rovó, Petra
last_name: Rovó
- first_name: Colin A.
full_name: Smith, Colin A.
last_name: Smith
- first_name: Diego
full_name: Gauto, Diego
last_name: Gauto
- first_name: Bert L.
full_name: de Groot, Bert L.
last_name: de Groot
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Rasmus
full_name: Linser, Rasmus
last_name: Linser
citation:
ama: Rovó P, Smith CA, Gauto D, de Groot BL, Schanda P, Linser R. Mechanistic insights
into microsecond time-scale motion of solid proteins using complementary 15N and
1H relaxation dispersion techniques. Journal of the American Chemical Society.
2019;141(2):858-869. doi:10.1021/jacs.8b09258
apa: Rovó, P., Smith, C. A., Gauto, D., de Groot, B. L., Schanda, P., & Linser,
R. (2019). Mechanistic insights into microsecond time-scale motion of solid proteins
using complementary 15N and 1H relaxation dispersion techniques. Journal of
the American Chemical Society. American Chemical Society. https://doi.org/10.1021/jacs.8b09258
chicago: Rovó, Petra, Colin A. Smith, Diego Gauto, Bert L. de Groot, Paul Schanda,
and Rasmus Linser. “Mechanistic Insights into Microsecond Time-Scale Motion of
Solid Proteins Using Complementary 15N and 1H Relaxation Dispersion Techniques.”
Journal of the American Chemical Society. American Chemical Society, 2019.
https://doi.org/10.1021/jacs.8b09258.
ieee: P. Rovó, C. A. Smith, D. Gauto, B. L. de Groot, P. Schanda, and R. Linser,
“Mechanistic insights into microsecond time-scale motion of solid proteins using
complementary 15N and 1H relaxation dispersion techniques,” Journal of the
American Chemical Society, vol. 141, no. 2. American Chemical Society, pp.
858–869, 2019.
ista: Rovó P, Smith CA, Gauto D, de Groot BL, Schanda P, Linser R. 2019. Mechanistic
insights into microsecond time-scale motion of solid proteins using complementary
15N and 1H relaxation dispersion techniques. Journal of the American Chemical
Society. 141(2), 858–869.
mla: Rovó, Petra, et al. “Mechanistic Insights into Microsecond Time-Scale Motion
of Solid Proteins Using Complementary 15N and 1H Relaxation Dispersion Techniques.”
Journal of the American Chemical Society, vol. 141, no. 2, American Chemical
Society, 2019, pp. 858–69, doi:10.1021/jacs.8b09258.
short: P. Rovó, C.A. Smith, D. Gauto, B.L. de Groot, P. Schanda, R. Linser, Journal
of the American Chemical Society 141 (2019) 858–869.
date_created: 2020-09-17T10:29:50Z
date_published: 2019-01-08T00:00:00Z
date_updated: 2021-01-12T08:19:07Z
day: '08'
doi: 10.1021/jacs.8b09258
extern: '1'
external_id:
pmid:
- '30620186'
intvolume: ' 141'
issue: '2'
keyword:
- Colloid and Surface Chemistry
- Biochemistry
- General Chemistry
- Catalysis
language:
- iso: eng
month: '01'
oa_version: Submitted Version
page: 858-869
pmid: 1
publication: Journal of the American Chemical Society
publication_identifier:
issn:
- 0002-7863
- 1520-5126
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
status: public
title: Mechanistic insights into microsecond time-scale motion of solid proteins using
complementary 15N and 1H relaxation dispersion techniques
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 141
year: '2019'
...
---
_id: '9060'
abstract:
- lang: eng
text: Molecular motors are essential to the living, generating fluctuations that
boost transport and assist assembly. Active colloids, that consume energy to move,
hold similar potential for man-made materials controlled by forces generated from
within. Yet, their use as a powerhouse in materials science lacks. Here we show
a massive acceleration of the annealing of a monolayer of passive beads by moderate
addition of self-propelled microparticles. We rationalize our observations with
a model of collisions that drive active fluctuations and activate the annealing.
The experiment is quantitatively compared with Brownian dynamic simulations that
further unveil a dynamical transition in the mechanism of annealing. Active dopants
travel uniformly in the system or co-localize at the grain boundaries as a result
of the persistence of their motion. Our findings uncover the potential of internal
activity to control materials and lay the groundwork for the rise of materials
science beyond equilibrium.
article_number: '3380'
article_processing_charge: No
article_type: original
arxiv: 1
author:
- first_name: Sophie
full_name: Ramananarivo, Sophie
last_name: Ramananarivo
- first_name: Etienne
full_name: Ducrot, Etienne
last_name: Ducrot
- first_name: Jérémie A
full_name: Palacci, Jérémie A
id: 8fb92548-2b22-11eb-b7c1-a3f0d08d7c7d
last_name: Palacci
orcid: 0000-0002-7253-9465
citation:
ama: Ramananarivo S, Ducrot E, Palacci JA. Activity-controlled annealing of colloidal
monolayers. Nature Communications. 2019;10(1). doi:10.1038/s41467-019-11362-y
apa: Ramananarivo, S., Ducrot, E., & Palacci, J. A. (2019). Activity-controlled
annealing of colloidal monolayers. Nature Communications. Springer Nature.
https://doi.org/10.1038/s41467-019-11362-y
chicago: Ramananarivo, Sophie, Etienne Ducrot, and Jérémie A Palacci. “Activity-Controlled
Annealing of Colloidal Monolayers.” Nature Communications. Springer Nature,
2019. https://doi.org/10.1038/s41467-019-11362-y.
ieee: S. Ramananarivo, E. Ducrot, and J. A. Palacci, “Activity-controlled annealing
of colloidal monolayers,” Nature Communications, vol. 10, no. 1. Springer
Nature, 2019.
ista: Ramananarivo S, Ducrot E, Palacci JA. 2019. Activity-controlled annealing
of colloidal monolayers. Nature Communications. 10(1), 3380.
mla: Ramananarivo, Sophie, et al. “Activity-Controlled Annealing of Colloidal Monolayers.”
Nature Communications, vol. 10, no. 1, 3380, Springer Nature, 2019, doi:10.1038/s41467-019-11362-y.
short: S. Ramananarivo, E. Ducrot, J.A. Palacci, Nature Communications 10 (2019).
date_created: 2021-02-02T13:43:36Z
date_published: 2019-07-29T00:00:00Z
date_updated: 2023-02-23T13:47:59Z
day: '29'
ddc:
- '530'
doi: 10.1038/s41467-019-11362-y
extern: '1'
external_id:
arxiv:
- '1909.07382'
pmid:
- '31358762'
file:
- access_level: open_access
checksum: 70c6e5d6fbea0932b0669505ab6633ec
content_type: application/pdf
creator: cziletti
date_created: 2021-02-02T13:47:21Z
date_updated: 2021-02-02T13:47:21Z
file_id: '9061'
file_name: 2019_NatureComm_Ramananarivo.pdf
file_size: 2820337
relation: main_file
success: 1
file_date_updated: 2021-02-02T13:47:21Z
has_accepted_license: '1'
intvolume: ' 10'
issue: '1'
keyword:
- General Biochemistry
- Genetics and Molecular Biology
- General Physics and Astronomy
- General Chemistry
language:
- iso: eng
month: '07'
oa: 1
oa_version: Published Version
pmid: 1
publication: Nature Communications
publication_identifier:
issn:
- 2041-1723
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: Activity-controlled annealing of colloidal monolayers
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: D865714E-FA4E-11E9-B85B-F5C5E5697425
volume: 10
year: '2019'
...
---
_id: '13374'
abstract:
- lang: eng
text: Confining molecules to volumes only slightly larger than the molecules themselves
can profoundly alter their properties. Molecular switches—entities that can be
toggled between two or more forms upon exposure to an external stimulus—often
require conformational freedom to isomerize. Therefore, placing these switches
in confined spaces can render them non-operational. To preserve the switchability
of these species under confinement, we work with a water-soluble coordination
cage that is flexible enough to adapt its shape to the conformation of the encapsulated
guest. We show that owing to its flexibility, the cage is not only capable of
accommodating—and solubilizing in water—several light-responsive spiropyran-based
molecular switches, but, more importantly, it also provides an environment suitable
for the efficient, reversible photoisomerization of the bound guests. Our findings
pave the way towards studying various molecular switching processes in confined
environments.
article_number: '641'
article_processing_charge: No
article_type: original
author:
- first_name: Dipak
full_name: Samanta, Dipak
last_name: Samanta
- first_name: Daria
full_name: Galaktionova, Daria
last_name: Galaktionova
- first_name: Julius
full_name: Gemen, Julius
last_name: Gemen
- first_name: Linda J. W.
full_name: Shimon, Linda J. W.
last_name: Shimon
- first_name: Yael
full_name: Diskin-Posner, Yael
last_name: Diskin-Posner
- first_name: Liat
full_name: Avram, Liat
last_name: Avram
- first_name: Petr
full_name: Král, Petr
last_name: Král
- first_name: Rafal
full_name: Klajn, Rafal
id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b
last_name: Klajn
citation:
ama: Samanta D, Galaktionova D, Gemen J, et al. Reversible chromism of spiropyran
in the cavity of a flexible coordination cage. Nature Communications. 2018;9.
doi:10.1038/s41467-017-02715-6
apa: Samanta, D., Galaktionova, D., Gemen, J., Shimon, L. J. W., Diskin-Posner,
Y., Avram, L., … Klajn, R. (2018). Reversible chromism of spiropyran in the cavity
of a flexible coordination cage. Nature Communications. Springer Nature.
https://doi.org/10.1038/s41467-017-02715-6
chicago: Samanta, Dipak, Daria Galaktionova, Julius Gemen, Linda J. W. Shimon, Yael
Diskin-Posner, Liat Avram, Petr Král, and Rafal Klajn. “Reversible Chromism of
Spiropyran in the Cavity of a Flexible Coordination Cage.” Nature Communications.
Springer Nature, 2018. https://doi.org/10.1038/s41467-017-02715-6.
ieee: D. Samanta et al., “Reversible chromism of spiropyran in the cavity
of a flexible coordination cage,” Nature Communications, vol. 9. Springer
Nature, 2018.
ista: Samanta D, Galaktionova D, Gemen J, Shimon LJW, Diskin-Posner Y, Avram L,
Král P, Klajn R. 2018. Reversible chromism of spiropyran in the cavity of a flexible
coordination cage. Nature Communications. 9, 641.
mla: Samanta, Dipak, et al. “Reversible Chromism of Spiropyran in the Cavity of
a Flexible Coordination Cage.” Nature Communications, vol. 9, 641, Springer
Nature, 2018, doi:10.1038/s41467-017-02715-6.
short: D. Samanta, D. Galaktionova, J. Gemen, L.J.W. Shimon, Y. Diskin-Posner, L.
Avram, P. Král, R. Klajn, Nature Communications 9 (2018).
date_created: 2023-08-01T09:39:32Z
date_published: 2018-02-13T00:00:00Z
date_updated: 2024-10-14T12:14:34Z
day: '13'
doi: 10.1038/s41467-017-02715-6
extern: '1'
external_id:
pmid:
- '29440687'
intvolume: ' 9'
keyword:
- General Physics and Astronomy
- General Biochemistry
- Genetics and Molecular Biology
- General Chemistry
- Multidisciplinary
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1038/s41467-017-02715-6
month: '02'
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/s41467-018-03701-2
scopus_import: '1'
status: public
title: Reversible chromism of spiropyran in the cavity of a flexible coordination
cage
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 9
year: '2018'
...
---
_id: '13377'
abstract:
- lang: eng
text: Confining organic molecules to the surfaces of inorganic nanoparticles can
induce intermolecular interactions between them, which can affect the composition
of the mixed self-assembled monolayers obtained by co-adsorption from solution
of two different molecules. Two thiolated ligands (a dialkylviologen and a zwitterionic
sulfobetaine) that can interact with each other electrostatically were coadsorbed
onto gold nanoparticles. The nanoparticles favor a narrow range of ratios of these
two molecules that is largely independent of the molar ratio in solution. Changing
the solution molar ratio of the two ligands by a factor of 5 000 affects the on-nanoparticle
ratio of these ligands by only threefold. This behavior is reminiscent of the
formation of insoluble inorganic salts (such as AgCl), which similarly compensate
positive and negative charges upon crystallizing. Our results pave the way towards
developing well-defined hybrid organic–inorganic nanostructures.
article_processing_charge: No
article_type: original
author:
- first_name: Zonglin
full_name: Chu, Zonglin
last_name: Chu
- first_name: Yanxiao
full_name: Han, Yanxiao
last_name: Han
- first_name: Petr
full_name: Král, Petr
last_name: Král
- first_name: Rafal
full_name: Klajn, Rafal
id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b
last_name: Klajn
citation:
ama: 'Chu Z, Han Y, Král P, Klajn R. “Precipitation on nanoparticles”: Attractive
intermolecular interactions stabilize specific ligand ratios on the surfaces of
nanoparticles. Angewandte Chemie International Edition. 2018;57(24):7023-7027.
doi:10.1002/anie.201800673'
apa: 'Chu, Z., Han, Y., Král, P., & Klajn, R. (2018). “Precipitation on nanoparticles”:
Attractive intermolecular interactions stabilize specific ligand ratios on the
surfaces of nanoparticles. Angewandte Chemie International Edition. Wiley.
https://doi.org/10.1002/anie.201800673'
chicago: 'Chu, Zonglin, Yanxiao Han, Petr Král, and Rafal Klajn. “‘Precipitation
on Nanoparticles’: Attractive Intermolecular Interactions Stabilize Specific Ligand
Ratios on the Surfaces of Nanoparticles.” Angewandte Chemie International Edition.
Wiley, 2018. https://doi.org/10.1002/anie.201800673.'
ieee: 'Z. Chu, Y. Han, P. Král, and R. Klajn, “‘Precipitation on nanoparticles’:
Attractive intermolecular interactions stabilize specific ligand ratios on the
surfaces of nanoparticles,” Angewandte Chemie International Edition, vol.
57, no. 24. Wiley, pp. 7023–7027, 2018.'
ista: 'Chu Z, Han Y, Král P, Klajn R. 2018. “Precipitation on nanoparticles”: Attractive
intermolecular interactions stabilize specific ligand ratios on the surfaces of
nanoparticles. Angewandte Chemie International Edition. 57(24), 7023–7027.'
mla: 'Chu, Zonglin, et al. “‘Precipitation on Nanoparticles’: Attractive Intermolecular
Interactions Stabilize Specific Ligand Ratios on the Surfaces of Nanoparticles.”
Angewandte Chemie International Edition, vol. 57, no. 24, Wiley, 2018,
pp. 7023–27, doi:10.1002/anie.201800673.'
short: Z. Chu, Y. Han, P. Král, R. Klajn, Angewandte Chemie International Edition
57 (2018) 7023–7027.
date_created: 2023-08-01T09:40:16Z
date_published: 2018-06-11T00:00:00Z
date_updated: 2024-10-14T12:15:04Z
day: '11'
doi: 10.1002/anie.201800673
extern: '1'
external_id:
pmid:
- '29673022'
intvolume: ' 57'
issue: '24'
keyword:
- General Chemistry
- Catalysis
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1002/anie.201800673
month: '06'
oa: 1
oa_version: Published Version
page: 7023-7027
pmid: 1
publication: Angewandte Chemie International Edition
publication_identifier:
eissn:
- 1521-3773
issn:
- 1433-7851
publication_status: published
publisher: Wiley
quality_controlled: '1'
scopus_import: '1'
status: public
title: '“Precipitation on nanoparticles”: Attractive intermolecular interactions stabilize
specific ligand ratios on the surfaces of nanoparticles'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 57
year: '2018'
...
---
_id: '14284'
abstract:
- lang: eng
text: Pore-forming toxins (PFT) are virulence factors that transform from soluble
to membrane-bound states. The Yersinia YaxAB system represents a family of binary
α-PFTs with orthologues in human, insect, and plant pathogens, with unknown structures.
YaxAB was shown to be cytotoxic and likely involved in pathogenesis, though the
molecular basis for its two-component lytic mechanism remains elusive. Here, we
present crystal structures of YaxA and YaxB, together with a cryo-electron microscopy
map of the YaxAB complex. Our structures reveal a pore predominantly composed
of decamers of YaxA–YaxB heterodimers. Both subunits bear membrane-active moieties,
but only YaxA is capable of binding to membranes by itself. YaxB can subsequently
be recruited to membrane-associated YaxA and induced to present its lytic transmembrane
helices. Pore formation can progress by further oligomerization of YaxA–YaxB dimers.
Our results allow for a comparison between pore assemblies belonging to the wider
ClyA-like family of α-PFTs, highlighting diverse pore architectures.
article_number: '1806'
article_processing_charge: No
article_type: original
author:
- first_name: Bastian
full_name: Bräuning, Bastian
last_name: Bräuning
- first_name: Eva
full_name: Bertosin, Eva
last_name: Bertosin
- first_name: Florian M
full_name: Praetorius, Florian M
id: dfec9381-4341-11ee-8fd8-faa02bba7d62
last_name: Praetorius
- first_name: Christian
full_name: Ihling, Christian
last_name: Ihling
- first_name: Alexandra
full_name: Schatt, Alexandra
last_name: Schatt
- first_name: Agnes
full_name: Adler, Agnes
last_name: Adler
- first_name: Klaus
full_name: Richter, Klaus
last_name: Richter
- first_name: Andrea
full_name: Sinz, Andrea
last_name: Sinz
- first_name: Hendrik
full_name: Dietz, Hendrik
last_name: Dietz
- first_name: Michael
full_name: Groll, Michael
last_name: Groll
citation:
ama: Bräuning B, Bertosin E, Praetorius FM, et al. Structure and mechanism of the
two-component α-helical pore-forming toxin YaxAB. Nature Communications.
2018;9. doi:10.1038/s41467-018-04139-2
apa: Bräuning, B., Bertosin, E., Praetorius, F. M., Ihling, C., Schatt, A., Adler,
A., … Groll, M. (2018). Structure and mechanism of the two-component α-helical
pore-forming toxin YaxAB. Nature Communications. Springer Nature. https://doi.org/10.1038/s41467-018-04139-2
chicago: Bräuning, Bastian, Eva Bertosin, Florian M Praetorius, Christian Ihling,
Alexandra Schatt, Agnes Adler, Klaus Richter, Andrea Sinz, Hendrik Dietz, and
Michael Groll. “Structure and Mechanism of the Two-Component α-Helical Pore-Forming
Toxin YaxAB.” Nature Communications. Springer Nature, 2018. https://doi.org/10.1038/s41467-018-04139-2.
ieee: B. Bräuning et al., “Structure and mechanism of the two-component α-helical
pore-forming toxin YaxAB,” Nature Communications, vol. 9. Springer Nature,
2018.
ista: Bräuning B, Bertosin E, Praetorius FM, Ihling C, Schatt A, Adler A, Richter
K, Sinz A, Dietz H, Groll M. 2018. Structure and mechanism of the two-component
α-helical pore-forming toxin YaxAB. Nature Communications. 9, 1806.
mla: Bräuning, Bastian, et al. “Structure and Mechanism of the Two-Component α-Helical
Pore-Forming Toxin YaxAB.” Nature Communications, vol. 9, 1806, Springer
Nature, 2018, doi:10.1038/s41467-018-04139-2.
short: B. Bräuning, E. Bertosin, F.M. Praetorius, C. Ihling, A. Schatt, A. Adler,
K. Richter, A. Sinz, H. Dietz, M. Groll, Nature Communications 9 (2018).
date_created: 2023-09-06T12:07:33Z
date_published: 2018-05-04T00:00:00Z
date_updated: 2023-11-07T11:46:12Z
day: '04'
doi: 10.1038/s41467-018-04139-2
extern: '1'
external_id:
pmid:
- '29728606'
intvolume: ' 9'
keyword:
- General Physics and Astronomy
- General Biochemistry
- Genetics and Molecular Biology
- General Chemistry
- Multidisciplinary
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1038/s41467-018-04139-2
month: '05'
oa: 1
oa_version: Published Version
pmid: 1
publication: Nature Communications
publication_identifier:
issn:
- 2041-1723
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 9
year: '2018'
...
---
_id: '15107'
article_processing_charge: No
article_type: review
author:
- first_name: Soumendu
full_name: Roy, Soumendu
last_name: Roy
- first_name: Sumit
full_name: Roy, Sumit
id: 67a1dc7d-cffb-11ee-b082-e15ca6a616d9
last_name: Roy
orcid: 0000-0002-6883-4939
- first_name: Anish
full_name: Rao, Anish
last_name: Rao
- first_name: Gayathri
full_name: Devatha, Gayathri
last_name: Devatha
- first_name: Pramod P.
full_name: Pillai, Pramod P.
last_name: Pillai
citation:
ama: Roy S, Roy S, Rao A, Devatha G, Pillai PP. Precise nanoparticle–reactant interaction
outplays ligand poisoning in visible-light photocatalysis. Chemistry of Materials.
2018;30(23):8415-8419. doi:10.1021/acs.chemmater.8b03108
apa: Roy, S., Roy, S., Rao, A., Devatha, G., & Pillai, P. P. (2018). Precise
nanoparticle–reactant interaction outplays ligand poisoning in visible-light photocatalysis.
Chemistry of Materials. American Chemical Society. https://doi.org/10.1021/acs.chemmater.8b03108
chicago: Roy, Soumendu, Sumit Roy, Anish Rao, Gayathri Devatha, and Pramod P. Pillai.
“Precise Nanoparticle–Reactant Interaction Outplays Ligand Poisoning in Visible-Light
Photocatalysis.” Chemistry of Materials. American Chemical Society, 2018.
https://doi.org/10.1021/acs.chemmater.8b03108.
ieee: S. Roy, S. Roy, A. Rao, G. Devatha, and P. P. Pillai, “Precise nanoparticle–reactant
interaction outplays ligand poisoning in visible-light photocatalysis,” Chemistry
of Materials, vol. 30, no. 23. American Chemical Society, pp. 8415–8419, 2018.
ista: Roy S, Roy S, Rao A, Devatha G, Pillai PP. 2018. Precise nanoparticle–reactant
interaction outplays ligand poisoning in visible-light photocatalysis. Chemistry
of Materials. 30(23), 8415–8419.
mla: Roy, Soumendu, et al. “Precise Nanoparticle–Reactant Interaction Outplays Ligand
Poisoning in Visible-Light Photocatalysis.” Chemistry of Materials, vol.
30, no. 23, American Chemical Society, 2018, pp. 8415–19, doi:10.1021/acs.chemmater.8b03108.
short: S. Roy, S. Roy, A. Rao, G. Devatha, P.P. Pillai, Chemistry of Materials 30
(2018) 8415–8419.
date_created: 2024-03-12T12:54:30Z
date_published: 2018-11-19T00:00:00Z
date_updated: 2024-03-20T07:50:07Z
day: '19'
doi: 10.1021/acs.chemmater.8b03108
extern: '1'
intvolume: ' 30'
issue: '23'
keyword:
- Materials Chemistry
- General Chemical Engineering
- General Chemistry
language:
- iso: eng
month: '11'
oa_version: None
page: 8415-8419
publication: Chemistry of Materials
publication_identifier:
eissn:
- 1520-5002
issn:
- 0897-4756
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Precise nanoparticle–reactant interaction outplays ligand poisoning in visible-light
photocatalysis
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 30
year: '2018'
...
---
_id: '10360'
abstract:
- lang: eng
text: Mapping free-energy landscapes has proved to be a powerful tool for studying
reaction mechanisms. Many complex biomolecular assembly processes, however, have
remained challenging to access using this approach, including the aggregation
of peptides and proteins into amyloid fibrils implicated in a range of disorders.
Here, we generalize the strategy used to probe free-energy landscapes in protein
folding to determine the activation energies and entropies that characterize each
of the molecular steps in the aggregation of the amyloid-β peptide (Aβ42), which
is associated with Alzheimer’s disease. Our results reveal that interactions between
monomeric Aβ42 and amyloid fibrils during fibril-dependent secondary nucleation
fundamentally reverse the thermodynamic signature of this process relative to
primary nucleation, even though both processes generate aggregates from soluble
peptides. By mapping the energetic and entropic contributions along the reaction
trajectories, we show that the catalytic efficiency of Aβ42 fibril surfaces results
from the enthalpic stabilization of adsorbing peptides in conformations amenable
to nucleation, resulting in a dramatic lowering of the activation energy for nucleation.
acknowledgement: We thank B. Jönsson and I. André for helpful discussions. We acknowledge
financial support from the Schiff Foundation (S.I.A.C.), St John’s College, Cambridge
(S.I.A.C.), the Royal Physiographic Society (R.C.), the Research School FLÄK of
Lund University (S.L., R.C.), the Swedish Research Council (S.L.) and its Linneaus
Centre Organizing Molecular Matter (S.L.), the Crafoord Foundation (S.L.), Alzheimerfonden
(S.L.), the European Research Council (S.L.), NanoLund (S.L.), Knut and Alice Wallenberg
Foundation (S.L.), Peterhouse, Cambridge (T.C.T.M.), the Swiss National Science
Foundation (T.C.T.M.), Magdalene College, Cambridge (A.K.B.), the Leverhulme Trust
(A.K.B.), the Royal Society (A.Š.), the Academy of Medical Sciences (A.Š.), the
Wellcome Trust (C.M.D., T.P.J.K., A.Š.), and the Centre for Misfolding Diseases
(C.M.D., T.P.J.K, M.V.). A.K.B. thanks the Alzheimer Forschung Initiative (AFI).
article_processing_charge: No
article_type: original
author:
- first_name: Samuel I. A.
full_name: Cohen, Samuel I. A.
last_name: Cohen
- first_name: Risto
full_name: Cukalevski, Risto
last_name: Cukalevski
- first_name: Thomas C. T.
full_name: Michaels, Thomas C. T.
last_name: Michaels
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Mattias
full_name: Törnquist, Mattias
last_name: Törnquist
- first_name: Michele
full_name: Vendruscolo, Michele
last_name: Vendruscolo
- first_name: Christopher M.
full_name: Dobson, Christopher M.
last_name: Dobson
- first_name: Alexander K.
full_name: Buell, Alexander K.
last_name: Buell
- first_name: Tuomas P. J.
full_name: Knowles, Tuomas P. J.
last_name: Knowles
- first_name: Sara
full_name: Linse, Sara
last_name: Linse
citation:
ama: Cohen SIA, Cukalevski R, Michaels TCT, et al. Distinct thermodynamic signatures
of oligomer generation in the aggregation of the amyloid-β peptide. Nature
Chemistry. 2018;10(5):523-531. doi:10.1038/s41557-018-0023-x
apa: Cohen, S. I. A., Cukalevski, R., Michaels, T. C. T., Šarić, A., Törnquist,
M., Vendruscolo, M., … Linse, S. (2018). Distinct thermodynamic signatures of
oligomer generation in the aggregation of the amyloid-β peptide. Nature Chemistry.
Springer Nature. https://doi.org/10.1038/s41557-018-0023-x
chicago: Cohen, Samuel I. A., Risto Cukalevski, Thomas C. T. Michaels, Anđela Šarić,
Mattias Törnquist, Michele Vendruscolo, Christopher M. Dobson, Alexander K. Buell,
Tuomas P. J. Knowles, and Sara Linse. “Distinct Thermodynamic Signatures of Oligomer
Generation in the Aggregation of the Amyloid-β Peptide.” Nature Chemistry.
Springer Nature, 2018. https://doi.org/10.1038/s41557-018-0023-x.
ieee: S. I. A. Cohen et al., “Distinct thermodynamic signatures of oligomer
generation in the aggregation of the amyloid-β peptide,” Nature Chemistry,
vol. 10, no. 5. Springer Nature, pp. 523–531, 2018.
ista: Cohen SIA, Cukalevski R, Michaels TCT, Šarić A, Törnquist M, Vendruscolo M,
Dobson CM, Buell AK, Knowles TPJ, Linse S. 2018. Distinct thermodynamic signatures
of oligomer generation in the aggregation of the amyloid-β peptide. Nature Chemistry.
10(5), 523–531.
mla: Cohen, Samuel I. A., et al. “Distinct Thermodynamic Signatures of Oligomer
Generation in the Aggregation of the Amyloid-β Peptide.” Nature Chemistry,
vol. 10, no. 5, Springer Nature, 2018, pp. 523–31, doi:10.1038/s41557-018-0023-x.
short: S.I.A. Cohen, R. Cukalevski, T.C.T. Michaels, A. Šarić, M. Törnquist, M.
Vendruscolo, C.M. Dobson, A.K. Buell, T.P.J. Knowles, S. Linse, Nature Chemistry
10 (2018) 523–531.
date_created: 2021-11-26T12:41:38Z
date_published: 2018-03-26T00:00:00Z
date_updated: 2021-11-26T15:14:00Z
day: '26'
doi: 10.1038/s41557-018-0023-x
extern: '1'
external_id:
pmid:
- '29581486'
intvolume: ' 10'
issue: '5'
keyword:
- general chemical engineering
- general chemistry
language:
- iso: eng
month: '03'
oa_version: None
page: 523-531
pmid: 1
publication: Nature Chemistry
publication_identifier:
eissn:
- 1755-4349
issn:
- 1755-4330
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: Distinct thermodynamic signatures of oligomer generation in the aggregation
of the amyloid-β peptide
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 10
year: '2018'
...
---
_id: '8442'
abstract:
- lang: eng
text: Membrane proteins perform a host of vital cellular functions. Deciphering
the molecular mechanisms whereby they fulfill these functions requires detailed
biophysical and structural investigations. Detergents have proven pivotal to extract
the protein from its native surroundings. Yet, they provide a milieu that departs
significantly from that of the biological membrane, to the extent that the structure,
the dynamics, and the interactions of membrane proteins in detergents may considerably
vary, as compared to the native environment. Understanding the impact of detergents
on membrane proteins is, therefore, crucial to assess the biological relevance
of results obtained in detergents. Here, we review the strengths and weaknesses
of alkyl phosphocholines (or foscholines), the most widely used detergent in solution-NMR
studies of membrane proteins. While this class of detergents is often successful
for membrane protein solubilization, a growing list of examples points to destabilizing
and denaturing properties, in particular for α-helical membrane proteins. Our
comprehensive analysis stresses the importance of stringent controls when working
with this class of detergents and when analyzing the structure and dynamics of
membrane proteins in alkyl phosphocholine detergents.
article_processing_charge: No
article_type: original
author:
- first_name: Christophe
full_name: Chipot, Christophe
last_name: Chipot
- first_name: François
full_name: Dehez, François
last_name: Dehez
- first_name: Jason R.
full_name: Schnell, Jason R.
last_name: Schnell
- first_name: Nicole
full_name: Zitzmann, Nicole
last_name: Zitzmann
- first_name: Eva
full_name: Pebay-Peyroula, Eva
last_name: Pebay-Peyroula
- first_name: Laurent J.
full_name: Catoire, Laurent J.
last_name: Catoire
- first_name: Bruno
full_name: Miroux, Bruno
last_name: Miroux
- first_name: Edmund R. S.
full_name: Kunji, Edmund R. S.
last_name: Kunji
- first_name: Gianluigi
full_name: Veglia, Gianluigi
last_name: Veglia
- first_name: Timothy A.
full_name: Cross, Timothy A.
last_name: Cross
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: 'Chipot C, Dehez F, Schnell JR, et al. Perturbations of native membrane protein
structure in alkyl phosphocholine detergents: A critical assessment of NMR and
biophysical studies. Chemical Reviews. 2018;118(7):3559-3607. doi:10.1021/acs.chemrev.7b00570'
apa: 'Chipot, C., Dehez, F., Schnell, J. R., Zitzmann, N., Pebay-Peyroula, E., Catoire,
L. J., … Schanda, P. (2018). Perturbations of native membrane protein structure
in alkyl phosphocholine detergents: A critical assessment of NMR and biophysical
studies. Chemical Reviews. American Chemical Society. https://doi.org/10.1021/acs.chemrev.7b00570'
chicago: 'Chipot, Christophe, François Dehez, Jason R. Schnell, Nicole Zitzmann,
Eva Pebay-Peyroula, Laurent J. Catoire, Bruno Miroux, et al. “Perturbations of
Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical
Assessment of NMR and Biophysical Studies.” Chemical Reviews. American
Chemical Society, 2018. https://doi.org/10.1021/acs.chemrev.7b00570.'
ieee: 'C. Chipot et al., “Perturbations of native membrane protein structure
in alkyl phosphocholine detergents: A critical assessment of NMR and biophysical
studies,” Chemical Reviews, vol. 118, no. 7. American Chemical Society,
pp. 3559–3607, 2018.'
ista: 'Chipot C, Dehez F, Schnell JR, Zitzmann N, Pebay-Peyroula E, Catoire LJ,
Miroux B, Kunji ERS, Veglia G, Cross TA, Schanda P. 2018. Perturbations of native
membrane protein structure in alkyl phosphocholine detergents: A critical assessment
of NMR and biophysical studies. Chemical Reviews. 118(7), 3559–3607.'
mla: 'Chipot, Christophe, et al. “Perturbations of Native Membrane Protein Structure
in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical
Studies.” Chemical Reviews, vol. 118, no. 7, American Chemical Society,
2018, pp. 3559–607, doi:10.1021/acs.chemrev.7b00570.'
short: C. Chipot, F. Dehez, J.R. Schnell, N. Zitzmann, E. Pebay-Peyroula, L.J. Catoire,
B. Miroux, E.R.S. Kunji, G. Veglia, T.A. Cross, P. Schanda, Chemical Reviews 118
(2018) 3559–3607.
date_created: 2020-09-18T10:05:35Z
date_published: 2018-02-28T00:00:00Z
date_updated: 2021-01-12T08:19:18Z
day: '28'
doi: 10.1021/acs.chemrev.7b00570
extern: '1'
intvolume: ' 118'
issue: '7'
keyword:
- General Chemistry
language:
- iso: eng
month: '02'
oa_version: None
page: 3559-3607
publication: Chemical Reviews
publication_identifier:
issn:
- 0009-2665
- 1520-6890
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
status: public
title: 'Perturbations of native membrane protein structure in alkyl phosphocholine
detergents: A critical assessment of NMR and biophysical studies'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 118
year: '2018'
...
---
_id: '9053'
abstract:
- lang: eng
text: The development of strategies to assemble microscopic machines from dissipative
building blocks are essential on the route to novel active materials. We recently
demonstrated the hierarchical self-assembly of phoretic microswimmers into self-spinning
microgears and their synchronization by diffusiophoretic interactions [Aubret
et al., Nat. Phys., 2018]. In this paper, we adopt a pedagogical approach and
expose our strategy to control self-assembly and build machines using phoretic
phenomena. We notably introduce Highly Inclined Laminated Optical sheets microscopy
(HILO) to image and characterize anisotropic and dynamic diffusiophoretic interactions,
which cannot be performed by conventional fluorescence microscopy. The dynamics
of a (haematite) photocatalytic material immersed in (hydrogen peroxide) fuel
under various illumination patterns is first described and quantitatively rationalized
by a model of diffusiophoresis, the migration of a colloidal particle in a concentration
gradient. It is further exploited to design phototactic microswimmers that direct
towards the high intensity of light, as a result of the reorientation of the haematite
in a light gradient. We finally show the assembly of self-spinning microgears
from colloidal microswimmers and carefully characterize the interactions using
HILO techniques. The results are compared with analytical and numerical predictions
and agree quantitatively, stressing the important role played by concentration
gradients induced by chemical activity to control and design interactions. Because
the approach described hereby is generic, this works paves the way for the rational
design of machines by controlling phoretic phenomena.
article_processing_charge: No
article_type: original
arxiv: 1
author:
- first_name: Antoine
full_name: Aubret, Antoine
last_name: Aubret
- first_name: Jérémie A
full_name: Palacci, Jérémie A
id: 8fb92548-2b22-11eb-b7c1-a3f0d08d7c7d
last_name: Palacci
orcid: 0000-0002-7253-9465
citation:
ama: Aubret A, Palacci JA. Diffusiophoretic design of self-spinning microgears from
colloidal microswimmers. Soft Matter. 2018;14(47):9577-9588. doi:10.1039/c8sm01760c
apa: Aubret, A., & Palacci, J. A. (2018). Diffusiophoretic design of self-spinning
microgears from colloidal microswimmers. Soft Matter. Royal Society of
Chemistry . https://doi.org/10.1039/c8sm01760c
chicago: Aubret, Antoine, and Jérémie A Palacci. “Diffusiophoretic Design of Self-Spinning
Microgears from Colloidal Microswimmers.” Soft Matter. Royal Society of
Chemistry , 2018. https://doi.org/10.1039/c8sm01760c.
ieee: A. Aubret and J. A. Palacci, “Diffusiophoretic design of self-spinning microgears
from colloidal microswimmers,” Soft Matter, vol. 14, no. 47. Royal Society
of Chemistry , pp. 9577–9588, 2018.
ista: Aubret A, Palacci JA. 2018. Diffusiophoretic design of self-spinning microgears
from colloidal microswimmers. Soft Matter. 14(47), 9577–9588.
mla: Aubret, Antoine, and Jérémie A. Palacci. “Diffusiophoretic Design of Self-Spinning
Microgears from Colloidal Microswimmers.” Soft Matter, vol. 14, no. 47,
Royal Society of Chemistry , 2018, pp. 9577–88, doi:10.1039/c8sm01760c.
short: A. Aubret, J.A. Palacci, Soft Matter 14 (2018) 9577–9588.
date_created: 2021-02-01T13:44:41Z
date_published: 2018-12-21T00:00:00Z
date_updated: 2023-02-23T13:47:43Z
day: '21'
doi: 10.1039/c8sm01760c
extern: '1'
external_id:
arxiv:
- '1909.11121'
pmid:
- '30456407'
intvolume: ' 14'
issue: '47'
keyword:
- General Chemistry
- Condensed Matter Physics
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://arxiv.org/abs/1909.11121
month: '12'
oa: 1
oa_version: Preprint
page: 9577-9588
pmid: 1
publication: Soft Matter
publication_identifier:
eissn:
- 1744-6848
issn:
- 1744-683X
publication_status: published
publisher: 'Royal Society of Chemistry '
quality_controlled: '1'
scopus_import: '1'
status: public
title: Diffusiophoretic design of self-spinning microgears from colloidal microswimmers
type: journal_article
user_id: D865714E-FA4E-11E9-B85B-F5C5E5697425
volume: 14
year: '2018'
...
---
_id: '11065'
abstract:
- lang: eng
text: Premature aging disorders provide an opportunity to study the mechanisms that
drive aging. In Hutchinson-Gilford progeria syndrome (HGPS), a mutant form of
the nuclear scaffold protein lamin A distorts nuclei and sequesters nuclear proteins.
We sought to investigate protein homeostasis in this disease. Here, we report
a widespread increase in protein turnover in HGPS-derived cells compared to normal
cells. We determine that global protein synthesis is elevated as a consequence
of activated nucleoli and enhanced ribosome biogenesis in HGPS-derived fibroblasts.
Depleting normal lamin A or inducing mutant lamin A expression are each sufficient
to drive nucleolar expansion. We further show that nucleolar size correlates with
donor age in primary fibroblasts derived from healthy individuals and that ribosomal
RNA production increases with age, indicating that nucleolar size and activity
can serve as aging biomarkers. While limiting ribosome biogenesis extends lifespan
in several systems, we show that increased ribosome biogenesis and activity are
a hallmark of premature aging.
article_number: '328'
article_processing_charge: No
article_type: original
author:
- first_name: Abigail
full_name: Buchwalter, Abigail
last_name: Buchwalter
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
citation:
ama: Buchwalter A, Hetzer M. Nucleolar expansion and elevated protein translation
in premature aging. Nature Communications. 2017;8. doi:10.1038/s41467-017-00322-z
apa: Buchwalter, A., & Hetzer, M. (2017). Nucleolar expansion and elevated protein
translation in premature aging. Nature Communications. Springer Nature.
https://doi.org/10.1038/s41467-017-00322-z
chicago: Buchwalter, Abigail, and Martin Hetzer. “Nucleolar Expansion and Elevated
Protein Translation in Premature Aging.” Nature Communications. Springer
Nature, 2017. https://doi.org/10.1038/s41467-017-00322-z.
ieee: A. Buchwalter and M. Hetzer, “Nucleolar expansion and elevated protein translation
in premature aging,” Nature Communications, vol. 8. Springer Nature, 2017.
ista: Buchwalter A, Hetzer M. 2017. Nucleolar expansion and elevated protein translation
in premature aging. Nature Communications. 8, 328.
mla: Buchwalter, Abigail, and Martin Hetzer. “Nucleolar Expansion and Elevated Protein
Translation in Premature Aging.” Nature Communications, vol. 8, 328, Springer
Nature, 2017, doi:10.1038/s41467-017-00322-z.
short: A. Buchwalter, M. Hetzer, Nature Communications 8 (2017).
date_created: 2022-04-07T07:45:50Z
date_published: 2017-08-30T00:00:00Z
date_updated: 2024-10-14T11:20:12Z
day: '30'
doi: 10.1038/s41467-017-00322-z
extern: '1'
external_id:
pmid:
- '28855503'
intvolume: ' 8'
keyword:
- General Physics and Astronomy
- General Biochemistry
- Genetics and Molecular Biology
- General Chemistry
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1038/s41467-017-00322-z
month: '08'
oa: 1
oa_version: Published Version
pmid: 1
publication: Nature Communications
publication_identifier:
issn:
- 2041-1723
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: Nucleolar expansion and elevated protein translation in premature aging
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 8
year: '2017'
...
---
_id: '13380'
abstract:
- lang: eng
text: Although dissipative self-assembly is ubiquitous in nature, where it gives
rise to structures and functions critical to life, examples of artificial systems
featuring this mode of self-assembly are rare. Here, we identify the presence
of ephemeral assemblies during seeded growth of gold nanoparticles. In this process,
hydrazine reduces Au(III) ions, which attach to the existing nanoparticles “seeds”.
The attachment is accompanied by a local increase in the concentration of a surfactant,
which therefore forms a bilayer on nanoparticle surfaces, inducing their assembly.
The resulting aggregates gradually disassemble as the surfactant concentration
throughout the solution equilibrates. The lifetimes of the out-of-equilibrium
aggregates depend on and can be controlled by the size of the constituent nanoparticles.
We demonstrate the utility of our out-of-equilibrium aggregates to form transient
reflective coatings on polar surfaces.
article_processing_charge: No
article_type: original
author:
- first_name: Michał
full_name: Sawczyk, Michał
last_name: Sawczyk
- first_name: Rafal
full_name: Klajn, Rafal
id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b
last_name: Klajn
citation:
ama: Sawczyk M, Klajn R. Out-of-equilibrium aggregates and coatings during seeded
growth of metallic nanoparticles. Journal of the American Chemical Society.
2017;139(49):17973-17978. doi:10.1021/jacs.7b09111
apa: Sawczyk, M., & Klajn, R. (2017). Out-of-equilibrium aggregates and coatings
during seeded growth of metallic nanoparticles. Journal of the American Chemical
Society. American Chemical Society. https://doi.org/10.1021/jacs.7b09111
chicago: Sawczyk, Michał, and Rafal Klajn. “Out-of-Equilibrium Aggregates and Coatings
during Seeded Growth of Metallic Nanoparticles.” Journal of the American Chemical
Society. American Chemical Society, 2017. https://doi.org/10.1021/jacs.7b09111.
ieee: M. Sawczyk and R. Klajn, “Out-of-equilibrium aggregates and coatings during
seeded growth of metallic nanoparticles,” Journal of the American Chemical
Society, vol. 139, no. 49. American Chemical Society, pp. 17973–17978, 2017.
ista: Sawczyk M, Klajn R. 2017. Out-of-equilibrium aggregates and coatings during
seeded growth of metallic nanoparticles. Journal of the American Chemical Society.
139(49), 17973–17978.
mla: Sawczyk, Michał, and Rafal Klajn. “Out-of-Equilibrium Aggregates and Coatings
during Seeded Growth of Metallic Nanoparticles.” Journal of the American Chemical
Society, vol. 139, no. 49, American Chemical Society, 2017, pp. 17973–78,
doi:10.1021/jacs.7b09111.
short: M. Sawczyk, R. Klajn, Journal of the American Chemical Society 139 (2017)
17973–17978.
date_created: 2023-08-01T09:41:01Z
date_published: 2017-12-01T00:00:00Z
date_updated: 2024-10-14T12:15:25Z
day: '01'
doi: 10.1021/jacs.7b09111
extern: '1'
external_id:
pmid:
- '29193964'
intvolume: ' 139'
issue: '49'
keyword:
- Colloid and Surface Chemistry
- Biochemistry
- General Chemistry
- Catalysis
language:
- iso: eng
month: '12'
oa_version: None
page: 17973-17978
pmid: 1
publication: Journal of the American Chemical Society
publication_identifier:
eissn:
- 1520-5126
issn:
- 0002-7863
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Out-of-equilibrium aggregates and coatings during seeded growth of metallic
nanoparticles
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 139
year: '2017'
...
---
_id: '13382'
article_processing_charge: No
article_type: letter_note
author:
- first_name: Jan H.
full_name: van Esch, Jan H.
last_name: van Esch
- first_name: Rafal
full_name: Klajn, Rafal
id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b
last_name: Klajn
- first_name: Sijbren
full_name: Otto, Sijbren
last_name: Otto
citation:
ama: van Esch JH, Klajn R, Otto S. Chemical systems out of equilibrium. Chemical
Society Reviews. 2017;46(18):5474-5475. doi:10.1039/c7cs90088k
apa: van Esch, J. H., Klajn, R., & Otto, S. (2017). Chemical systems out of
equilibrium. Chemical Society Reviews. Royal Society of Chemistry. https://doi.org/10.1039/c7cs90088k
chicago: Esch, Jan H. van, Rafal Klajn, and Sijbren Otto. “Chemical Systems out
of Equilibrium.” Chemical Society Reviews. Royal Society of Chemistry,
2017. https://doi.org/10.1039/c7cs90088k.
ieee: J. H. van Esch, R. Klajn, and S. Otto, “Chemical systems out of equilibrium,”
Chemical Society Reviews, vol. 46, no. 18. Royal Society of Chemistry,
pp. 5474–5475, 2017.
ista: van Esch JH, Klajn R, Otto S. 2017. Chemical systems out of equilibrium. Chemical
Society Reviews. 46(18), 5474–5475.
mla: van Esch, Jan H., et al. “Chemical Systems out of Equilibrium.” Chemical
Society Reviews, vol. 46, no. 18, Royal Society of Chemistry, 2017, pp. 5474–75,
doi:10.1039/c7cs90088k.
short: J.H. van Esch, R. Klajn, S. Otto, Chemical Society Reviews 46 (2017) 5474–5475.
date_created: 2023-08-01T09:41:30Z
date_published: 2017-09-08T00:00:00Z
date_updated: 2024-10-14T12:15:48Z
day: '08'
doi: 10.1039/c7cs90088k
extern: '1'
external_id:
pmid:
- '28884760'
intvolume: ' 46'
issue: '18'
keyword:
- General Chemistry
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1039/c7cs90088k
month: '09'
oa: 1
oa_version: Published Version
page: 5474-5475
pmid: 1
publication: Chemical Society Reviews
publication_identifier:
eissn:
- 1460-4744
issn:
- 0306-0012
publication_status: published
publisher: Royal Society of Chemistry
quality_controlled: '1'
scopus_import: '1'
status: public
title: Chemical systems out of equilibrium
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 46
year: '2017'
...
---
_id: '14005'
abstract:
- lang: eng
text: Strong-field photoelectron holography and laser-induced electron diffraction
(LIED) are two powerful emerging methods for probing the ultrafast dynamics of
molecules. However, both of them have remained restricted to static systems and
to nuclear dynamics induced by strong-field ionization. Here we extend these promising
methods to image purely electronic valence-shell dynamics in molecules using photoelectron
holography. In the same experiment, we use LIED and photoelectron holography simultaneously,
to observe coupled electronic-rotational dynamics taking place on similar timescales.
These results offer perspectives for imaging ultrafast dynamics of molecules on
femtosecond to attosecond timescales.
article_number: '15651'
article_processing_charge: No
article_type: original
author:
- first_name: Samuel G.
full_name: Walt, Samuel G.
last_name: Walt
- first_name: Niraghatam
full_name: Bhargava Ram, Niraghatam
last_name: Bhargava Ram
- first_name: Marcos
full_name: Atala, Marcos
last_name: Atala
- first_name: Nikolay I
full_name: Shvetsov-Shilovski, Nikolay I
last_name: Shvetsov-Shilovski
- first_name: Aaron
full_name: von Conta, Aaron
last_name: von Conta
- first_name: Denitsa Rangelova
full_name: Baykusheva, Denitsa Rangelova
id: 71b4d059-2a03-11ee-914d-dfa3beed6530
last_name: Baykusheva
- first_name: Manfred
full_name: Lein, Manfred
last_name: Lein
- first_name: Hans Jakob
full_name: Wörner, Hans Jakob
last_name: Wörner
citation:
ama: Walt SG, Bhargava Ram N, Atala M, et al. Dynamics of valence-shell electrons
and nuclei probed by strong-field holography and rescattering. Nature Communications.
2017;8. doi:10.1038/ncomms15651
apa: Walt, S. G., Bhargava Ram, N., Atala, M., Shvetsov-Shilovski, N. I., von Conta,
A., Baykusheva, D. R., … Wörner, H. J. (2017). Dynamics of valence-shell electrons
and nuclei probed by strong-field holography and rescattering. Nature Communications.
Springer Nature. https://doi.org/10.1038/ncomms15651
chicago: Walt, Samuel G., Niraghatam Bhargava Ram, Marcos Atala, Nikolay I Shvetsov-Shilovski,
Aaron von Conta, Denitsa Rangelova Baykusheva, Manfred Lein, and Hans Jakob Wörner.
“Dynamics of Valence-Shell Electrons and Nuclei Probed by Strong-Field Holography
and Rescattering.” Nature Communications. Springer Nature, 2017. https://doi.org/10.1038/ncomms15651.
ieee: S. G. Walt et al., “Dynamics of valence-shell electrons and nuclei
probed by strong-field holography and rescattering,” Nature Communications,
vol. 8. Springer Nature, 2017.
ista: Walt SG, Bhargava Ram N, Atala M, Shvetsov-Shilovski NI, von Conta A, Baykusheva
DR, Lein M, Wörner HJ. 2017. Dynamics of valence-shell electrons and nuclei probed
by strong-field holography and rescattering. Nature Communications. 8, 15651.
mla: Walt, Samuel G., et al. “Dynamics of Valence-Shell Electrons and Nuclei Probed
by Strong-Field Holography and Rescattering.” Nature Communications, vol.
8, 15651, Springer Nature, 2017, doi:10.1038/ncomms15651.
short: S.G. Walt, N. Bhargava Ram, M. Atala, N.I. Shvetsov-Shilovski, A. von Conta,
D.R. Baykusheva, M. Lein, H.J. Wörner, Nature Communications 8 (2017).
date_created: 2023-08-10T06:36:09Z
date_published: 2017-06-15T00:00:00Z
date_updated: 2023-08-22T08:26:06Z
day: '15'
doi: 10.1038/ncomms15651
extern: '1'
external_id:
pmid:
- '28643771'
intvolume: ' 8'
keyword:
- General Physics and Astronomy
- General Biochemistry
- Genetics and Molecular Biology
- General Chemistry
- Multidisciplinary
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1038/ncomms15651
month: '06'
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'
scopus_import: '1'
status: public
title: Dynamics of valence-shell electrons and nuclei probed by strong-field holography
and rescattering
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 8
year: '2017'
...
---
_id: '10369'
abstract:
- lang: eng
text: Biological membranes have a central role in mediating the organization of
membrane-curving proteins, a dynamic process that has proven to be challenging
to probe experimentally. Using atomic force microscopy, we capture the hierarchically
organized assemblies of Bin/amphiphysin/Rvs (BAR) proteins on supported lipid
membranes. Their structure reveals distinct long linear aggregates of proteins,
regularly spaced by up to 300 nm. Employing accurate free-energy calculations
from large-scale coarse-grained computer simulations, we found that the membrane
mediates the interaction among protein filaments as a combination of short- and
long-ranged interactions. The long-ranged component acts at strikingly long distances,
giving rise to a variety of micron-sized ordered patterns. This mechanism may
contribute to the long-ranged spatiotemporal control of membrane remodeling by
proteins in the cell.
acknowledgement: M.S. and G.A.V. acknowledge their research reported in this publication
as being supported by the National Institute of General Medical Sciences of the
National Institutes of Health under Award Number R01-GM063796. Computational resources
were provided to M.S. and G.A.V. by the National Science Foundation through XSEDE
(Grant TG-MCA94P017, supercomputers Stampede and Gordon), and also by the Blue Waters
computing project at the National Center for Supercomputing Applications (University
of Illinois at Urbana–Champaign, NSF Awards OCI-0725070 and ACI-1238993). A.Š. acknowledges
support from the Human Frontier Science Program and Royal Society. J.M.H. and K.Y.C.L.
acknowledge the support from the National Science Foundation (Grant MCB-1413613)
and the NSF-supported MRSEC program at the University of Chicago (Grant DMR-1420709).
We are grateful to Carsten Mim and Vinzenz Unger of Northwestern University for
generously providing us with the protein. We thank all the members of the Voth group
for fruitful discussions, especially John M. A. Grime.
article_processing_charge: No
article_type: original
author:
- first_name: Mijo
full_name: Simunovic, Mijo
last_name: Simunovic
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: J. Michael
full_name: Henderson, J. Michael
last_name: Henderson
- first_name: Ka Yee C.
full_name: Lee, Ka Yee C.
last_name: Lee
- first_name: Gregory A.
full_name: Voth, Gregory A.
last_name: Voth
citation:
ama: Simunovic M, Šarić A, Henderson JM, Lee KYC, Voth GA. Long-range organization
of membrane-curving proteins. ACS Central Science. 2017;3(12):1246-1253.
doi:10.1021/acscentsci.7b00392
apa: Simunovic, M., Šarić, A., Henderson, J. M., Lee, K. Y. C., & Voth, G. A.
(2017). Long-range organization of membrane-curving proteins. ACS Central Science.
American Chemical Society. https://doi.org/10.1021/acscentsci.7b00392
chicago: Simunovic, Mijo, Anđela Šarić, J. Michael Henderson, Ka Yee C. Lee, and
Gregory A. Voth. “Long-Range Organization of Membrane-Curving Proteins.” ACS
Central Science. American Chemical Society, 2017. https://doi.org/10.1021/acscentsci.7b00392.
ieee: M. Simunovic, A. Šarić, J. M. Henderson, K. Y. C. Lee, and G. A. Voth, “Long-range
organization of membrane-curving proteins,” ACS Central Science, vol. 3,
no. 12. American Chemical Society, pp. 1246–1253, 2017.
ista: Simunovic M, Šarić A, Henderson JM, Lee KYC, Voth GA. 2017. Long-range organization
of membrane-curving proteins. ACS Central Science. 3(12), 1246–1253.
mla: Simunovic, Mijo, et al. “Long-Range Organization of Membrane-Curving Proteins.”
ACS Central Science, vol. 3, no. 12, American Chemical Society, 2017, pp.
1246–53, doi:10.1021/acscentsci.7b00392.
short: M. Simunovic, A. Šarić, J.M. Henderson, K.Y.C. Lee, G.A. Voth, ACS Central
Science 3 (2017) 1246–1253.
date_created: 2021-11-29T08:49:50Z
date_published: 2017-11-21T00:00:00Z
date_updated: 2021-11-29T09:28:06Z
day: '21'
ddc:
- '540'
doi: 10.1021/acscentsci.7b00392
extern: '1'
external_id:
pmid:
- '29296664'
file:
- access_level: open_access
checksum: 1cf3e5e5342f2d728f47560acc3ec560
content_type: application/pdf
creator: cchlebak
date_created: 2021-11-29T09:00:40Z
date_updated: 2021-11-29T09:00:40Z
file_id: '10371'
file_name: 2017_ACSCentSci_Simunovic.pdf
file_size: 2635263
relation: main_file
success: 1
file_date_updated: 2021-11-29T09:00:40Z
has_accepted_license: '1'
intvolume: ' 3'
issue: '12'
keyword:
- general chemical engineering
- general chemistry
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://pubs.acs.org/doi/10.1021/acscentsci.7b00392
month: '11'
oa: 1
oa_version: Published Version
page: 1246-1253
pmid: 1
publication: ACS Central Science
publication_identifier:
eissn:
- 2374-7951
issn:
- 2374-7943
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Long-range organization of membrane-curving proteins
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: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 3
year: '2017'
...
---
_id: '10374'
abstract:
- lang: eng
text: The formation of filaments from naturally occurring protein molecules is a
process at the core of a range of functional and aberrant biological phenomena,
such as the assembly of the cytoskeleton or the appearance of aggregates in Alzheimer's
disease. The macroscopic behaviour associated with such processes is remarkably
diverse, ranging from simple nucleated growth to highly cooperative processes
with a well-defined lagtime. Thus, conventionally, different molecular mechanisms
have been used to explain the self-assembly of different proteins. Here we show
that this range of behaviour can be quantitatively captured by a single unifying
Petri net that describes filamentous growth in terms of aggregate number and aggregate
mass concentrations. By considering general features associated with a particular
network connectivity, we are able to establish directly the rate-determining steps
of the overall aggregation reaction from the system's scaling behaviour. We illustrate
the power of this framework on a range of different experimental and simulated
aggregating systems. The approach is general and will be applicable to any future
extensions of the reaction network of filamentous self-assembly.
acknowledgement: The research leading to these results has received funding from the
European Research Council under the European Union's Seventh Framework Programme
(FP7/2007-2013) through the ERC grant PhysProt (agreement no. 337969) (SL, TPJK),
Sidney Sussex College Cambridge (GM), the Frances and Augusta Newman Foundation
(TPJK), the Biotechnology and Biological Science Research Council (TPJK), the Swedish
Research Council (SL), the Academy of Medical Sciences (AŠ), Wellcome Trust (AŠ),
and the Cambridge Centre for Misfolding Diseases (CMD, TPJK, MV).
article_processing_charge: No
article_type: original
author:
- first_name: Georg
full_name: Meisl, Georg
last_name: Meisl
- first_name: Luke
full_name: Rajah, Luke
last_name: Rajah
- first_name: Samuel A. I.
full_name: Cohen, Samuel A. I.
last_name: Cohen
- first_name: Manuela
full_name: Pfammatter, Manuela
last_name: Pfammatter
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Erik
full_name: Hellstrand, Erik
last_name: Hellstrand
- first_name: Alexander K.
full_name: Buell, Alexander K.
last_name: Buell
- first_name: Adriano
full_name: Aguzzi, Adriano
last_name: Aguzzi
- first_name: Sara
full_name: Linse, Sara
last_name: Linse
- first_name: Michele
full_name: Vendruscolo, Michele
last_name: Vendruscolo
- first_name: Christopher M.
full_name: Dobson, Christopher M.
last_name: Dobson
- first_name: Tuomas P. J.
full_name: Knowles, Tuomas P. J.
last_name: Knowles
citation:
ama: Meisl G, Rajah L, Cohen SAI, et al. Scaling behaviour and rate-determining
steps in filamentous self-assembly. Chemical Science. 2017;8(10):7087-7097.
doi:10.1039/c7sc01965c
apa: Meisl, G., Rajah, L., Cohen, S. A. I., Pfammatter, M., Šarić, A., Hellstrand,
E., … Knowles, T. P. J. (2017). Scaling behaviour and rate-determining steps in
filamentous self-assembly. Chemical Science. Royal Society of Chemistry.
https://doi.org/10.1039/c7sc01965c
chicago: Meisl, Georg, Luke Rajah, Samuel A. I. Cohen, Manuela Pfammatter, Anđela
Šarić, Erik Hellstrand, Alexander K. Buell, et al. “Scaling Behaviour and Rate-Determining
Steps in Filamentous Self-Assembly.” Chemical Science. Royal Society of
Chemistry, 2017. https://doi.org/10.1039/c7sc01965c.
ieee: G. Meisl et al., “Scaling behaviour and rate-determining steps in filamentous
self-assembly,” Chemical Science, vol. 8, no. 10. Royal Society of Chemistry,
pp. 7087–7097, 2017.
ista: Meisl G, Rajah L, Cohen SAI, Pfammatter M, Šarić A, Hellstrand E, Buell AK,
Aguzzi A, Linse S, Vendruscolo M, Dobson CM, Knowles TPJ. 2017. Scaling behaviour
and rate-determining steps in filamentous self-assembly. Chemical Science. 8(10),
7087–7097.
mla: Meisl, Georg, et al. “Scaling Behaviour and Rate-Determining Steps in Filamentous
Self-Assembly.” Chemical Science, vol. 8, no. 10, Royal Society of Chemistry,
2017, pp. 7087–97, doi:10.1039/c7sc01965c.
short: G. Meisl, L. Rajah, S.A.I. Cohen, M. Pfammatter, A. Šarić, E. Hellstrand,
A.K. Buell, A. Aguzzi, S. Linse, M. Vendruscolo, C.M. Dobson, T.P.J. Knowles,
Chemical Science 8 (2017) 7087–7097.
date_created: 2021-11-29T09:29:31Z
date_published: 2017-08-31T00:00:00Z
date_updated: 2021-11-29T10:00:00Z
day: '31'
ddc:
- '540'
doi: 10.1039/c7sc01965c
extern: '1'
external_id:
pmid:
- '29147538'
intvolume: ' 8'
issue: '10'
keyword:
- general chemistry
language:
- iso: eng
license: https://creativecommons.org/licenses/by-nc/3.0/
main_file_link:
- open_access: '1'
url: https://pubs.rsc.org/en/content/articlelanding/2017/SC/C7SC01965C
month: '08'
oa: 1
oa_version: Published Version
page: 7087-7097
pmid: 1
publication: Chemical Science
publication_identifier:
eissn:
- 2041-6539
issn:
- 2041-6520
publication_status: published
publisher: Royal Society of Chemistry
quality_controlled: '1'
scopus_import: '1'
status: public
title: Scaling behaviour and rate-determining steps in filamentous self-assembly
tmp:
image: /images/cc_by_nc.png
legal_code_url: https://creativecommons.org/licenses/by-nc/3.0/legalcode
name: Creative Commons Attribution-NonCommercial 3.0 Unported (CC BY-NC 3.0)
short: CC BY-NC (3.0)
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 8
year: '2017'
...
---
_id: '10375'
abstract:
- lang: eng
text: 'Cellular membranes exhibit a large variety of shapes, strongly coupled to
their function. Many biological processes involve dynamic reshaping of membranes,
usually mediated by proteins. This interaction works both ways: while proteins
influence the membrane shape, the membrane shape affects the interactions between
the proteins. To study these membrane-mediated interactions on closed and anisotropically
curved membranes, we use colloids adhered to ellipsoidal membrane vesicles as
a model system. We find that two particles on a closed system always attract each
other, and tend to align with the direction of largest curvature. Multiple particles
form arcs, or, at large enough numbers, a complete ring surrounding the vesicle
in its equatorial plane. The resulting vesicle shape resembles a snowman. Our
results indicate that these physical interactions on membranes with anisotropic
shapes can be exploited by cells to drive macromolecules to preferred regions
of cellular or intracellular membranes, and utilized to initiate dynamic processes
such as cell division. The same principle could be used to find the midplane of
an artificial vesicle, as a first step towards dividing it into two equal parts.'
acknowledgement: This work was supported by the Netherlands Organisation for Scientific
Research (NWO/OCW), as part of the Frontiers of Nanoscience program.
article_processing_charge: No
article_type: original
arxiv: 1
author:
- first_name: Afshin
full_name: Vahid, Afshin
last_name: Vahid
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Timon
full_name: Idema, Timon
last_name: Idema
citation:
ama: Vahid A, Šarić A, Idema T. Curvature variation controls particle aggregation
on fluid vesicles. Soft Matter. 2017;13(28):4924-4930. doi:10.1039/c7sm00433h
apa: Vahid, A., Šarić, A., & Idema, T. (2017). Curvature variation controls
particle aggregation on fluid vesicles. Soft Matter. Royal Society of Chemistry.
https://doi.org/10.1039/c7sm00433h
chicago: Vahid, Afshin, Anđela Šarić, and Timon Idema. “Curvature Variation Controls
Particle Aggregation on Fluid Vesicles.” Soft Matter. Royal Society of
Chemistry, 2017. https://doi.org/10.1039/c7sm00433h.
ieee: A. Vahid, A. Šarić, and T. Idema, “Curvature variation controls particle aggregation
on fluid vesicles,” Soft Matter, vol. 13, no. 28. Royal Society of Chemistry,
pp. 4924–4930, 2017.
ista: Vahid A, Šarić A, Idema T. 2017. Curvature variation controls particle aggregation
on fluid vesicles. Soft Matter. 13(28), 4924–4930.
mla: Vahid, Afshin, et al. “Curvature Variation Controls Particle Aggregation on
Fluid Vesicles.” Soft Matter, vol. 13, no. 28, Royal Society of Chemistry,
2017, pp. 4924–30, doi:10.1039/c7sm00433h.
short: A. Vahid, A. Šarić, T. Idema, Soft Matter 13 (2017) 4924–4930.
date_created: 2021-11-29T10:00:39Z
date_published: 2017-06-15T00:00:00Z
date_updated: 2021-11-29T10:33:36Z
day: '15'
doi: 10.1039/c7sm00433h
extern: '1'
external_id:
arxiv:
- '1703.00776'
pmid:
- '28677712'
intvolume: ' 13'
issue: '28'
keyword:
- condensed matter physics
- general chemistry
language:
- iso: eng
license: https://creativecommons.org/licenses/by/3.0/
main_file_link:
- open_access: '1'
url: https://pubs.rsc.org/en/content/articlelanding/2017/SM/C7SM00433H
month: '06'
oa: 1
oa_version: Published Version
page: 4924-4930
pmid: 1
publication: Soft Matter
publication_identifier:
eissn:
- 1744-6848
issn:
- 1744-683X
publication_status: published
publisher: Royal Society of Chemistry
quality_controlled: '1'
scopus_import: '1'
status: public
title: Curvature variation controls particle aggregation on fluid vesicles
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/3.0/legalcode
name: Creative Commons Attribution 3.0 Unported (CC BY 3.0)
short: CC BY (3.0)
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 13
year: '2017'
...
---
_id: '8447'
abstract:
- lang: eng
text: 'Solid-state NMR spectroscopy can provide site-resolved information about
protein dynamics over many time scales. Here we combine protein deuteration, fast
magic-angle spinning (~45–60 kHz) and proton detection to study dynamics of ubiquitin
in microcrystals, and in particular a mutant in a region that undergoes microsecond
motions in a β-turn region in the wild-type protein. We use 15N R1ρ relaxation
measurements as a function of the radio-frequency (RF) field strength, i.e. relaxation
dispersion, to probe how the G53A mutation alters these dynamics. We report a
population-inversion of conformational states: the conformation that in the wild-type
protein is populated only sparsely becomes the predominant state. We furthermore
explore the potential to use amide-1H R1ρ relaxation to obtain insight into dynamics.
We show that while quantitative interpretation of 1H relaxation remains beyond
reach under the experimental conditions, due to coherent contributions to decay,
one may extract qualitative information about flexibility.'
article_processing_charge: No
article_type: original
author:
- first_name: Diego F.
full_name: Gauto, Diego F.
last_name: Gauto
- first_name: Audrey
full_name: Hessel, Audrey
last_name: Hessel
- first_name: Petra
full_name: Rovó, Petra
last_name: Rovó
- first_name: Vilius
full_name: Kurauskas, Vilius
last_name: Kurauskas
- first_name: Rasmus
full_name: Linser, Rasmus
last_name: Linser
- 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, Hessel A, Rovó P, Kurauskas V, Linser R, Schanda P. Protein conformational
dynamics studied by 15N and 1HR1ρ relaxation dispersion: Application to wild-type
and G53A ubiquitin crystals. Solid State Nuclear Magnetic Resonance. 2017;87(10):86-95.
doi:10.1016/j.ssnmr.2017.04.002'
apa: 'Gauto, D. F., Hessel, A., Rovó, P., Kurauskas, V., Linser, R., & Schanda,
P. (2017). Protein conformational dynamics studied by 15N and 1HR1ρ relaxation
dispersion: Application to wild-type and G53A ubiquitin crystals. Solid State
Nuclear Magnetic Resonance. Elsevier. https://doi.org/10.1016/j.ssnmr.2017.04.002'
chicago: 'Gauto, Diego F., Audrey Hessel, Petra Rovó, Vilius Kurauskas, Rasmus Linser,
and Paul Schanda. “Protein Conformational Dynamics Studied by 15N and 1HR1ρ Relaxation
Dispersion: Application to Wild-Type and G53A Ubiquitin Crystals.” Solid State
Nuclear Magnetic Resonance. Elsevier, 2017. https://doi.org/10.1016/j.ssnmr.2017.04.002.'
ieee: 'D. F. Gauto, A. Hessel, P. Rovó, V. Kurauskas, R. Linser, and P. Schanda,
“Protein conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion:
Application to wild-type and G53A ubiquitin crystals,” Solid State Nuclear
Magnetic Resonance, vol. 87, no. 10. Elsevier, pp. 86–95, 2017.'
ista: 'Gauto DF, Hessel A, Rovó P, Kurauskas V, Linser R, Schanda P. 2017. Protein
conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion: Application
to wild-type and G53A ubiquitin crystals. Solid State Nuclear Magnetic Resonance.
87(10), 86–95.'
mla: 'Gauto, Diego F., et al. “Protein Conformational Dynamics Studied by 15N and
1HR1ρ Relaxation Dispersion: Application to Wild-Type and G53A Ubiquitin Crystals.”
Solid State Nuclear Magnetic Resonance, vol. 87, no. 10, Elsevier, 2017,
pp. 86–95, doi:10.1016/j.ssnmr.2017.04.002.'
short: D.F. Gauto, A. Hessel, P. Rovó, V. Kurauskas, R. Linser, P. Schanda, Solid
State Nuclear Magnetic Resonance 87 (2017) 86–95.
date_created: 2020-09-18T10:06:18Z
date_published: 2017-10-01T00:00:00Z
date_updated: 2021-01-12T08:19:20Z
day: '01'
doi: 10.1016/j.ssnmr.2017.04.002
extern: '1'
intvolume: ' 87'
issue: '10'
keyword:
- Nuclear and High Energy Physics
- Instrumentation
- General Chemistry
- Radiation
language:
- iso: eng
month: '10'
oa_version: None
page: 86-95
publication: Solid State Nuclear Magnetic Resonance
publication_identifier:
issn:
- 0926-2040
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: 'Protein conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion:
Application to wild-type and G53A ubiquitin crystals'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 87
year: '2017'
...