---
_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: '8458'
abstract:
- lang: eng
text: The maintenance of bacterial cell shape and integrity is largely attributed
to peptidoglycan, a highly cross-linked biopolymer. The transpeptidases that perform
this cross-linking are important targets for antibiotics. Despite this biomedical
importance, to date no structure of a protein in complex with an intact bacterial
peptidoglycan has been resolved, primarily due to the large size and flexibility
of peptidoglycan sacculi. Here we use solid-state NMR spectroscopy to derive for
the first time an atomic model of an l,d-transpeptidase from Bacillus subtilis
bound to its natural substrate, the intact B. subtilis peptidoglycan. Importantly,
the model obtained from protein chemical shift perturbation data shows that both
domains—the catalytic domain as well as the proposed peptidoglycan recognition
domain—are important for the interaction and reveals a novel binding motif that
involves residues outside of the classical enzymatic pocket. Experiments on mutants
and truncated protein constructs independently confirm the binding site and the
implication of both domains. Through measurements of dipolar-coupling derived
order parameters of bond motion we show that protein binding reduces the flexibility
of peptidoglycan. This first report of an atomic model of a protein–peptidoglycan
complex paves the way for the design of new antibiotic drugs targeting l,d-transpeptidases.
The strategy developed here can be extended to the study of a large variety of
enzymes involved in peptidoglycan morphogenesis.
article_processing_charge: No
article_type: original
author:
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Sébastien
full_name: Triboulet, Sébastien
last_name: Triboulet
- first_name: Cédric
full_name: Laguri, Cédric
last_name: Laguri
- first_name: Catherine M.
full_name: Bougault, Catherine M.
last_name: Bougault
- first_name: Isabel
full_name: Ayala, Isabel
last_name: Ayala
- first_name: Morgane
full_name: Callon, Morgane
last_name: Callon
- first_name: Michel
full_name: Arthur, Michel
last_name: Arthur
- first_name: Jean-Pierre
full_name: Simorre, Jean-Pierre
last_name: Simorre
citation:
ama: Schanda P, Triboulet S, Laguri C, et al. Atomic model of a cell-wall cross-linking
enzyme in complex with an intact bacterial peptidoglycan. Journal of the American
Chemical Society. 2014;136(51):17852-17860. doi:10.1021/ja5105987
apa: Schanda, P., Triboulet, S., Laguri, C., Bougault, C. M., Ayala, I., Callon,
M., … Simorre, J.-P. (2014). Atomic model of a cell-wall cross-linking enzyme
in complex with an intact bacterial peptidoglycan. Journal of the American
Chemical Society. American Chemical Society. https://doi.org/10.1021/ja5105987
chicago: Schanda, Paul, Sébastien Triboulet, Cédric Laguri, Catherine M. Bougault,
Isabel Ayala, Morgane Callon, Michel Arthur, and Jean-Pierre Simorre. “Atomic
Model of a Cell-Wall Cross-Linking Enzyme in Complex with an Intact Bacterial
Peptidoglycan.” Journal of the American Chemical Society. American Chemical
Society, 2014. https://doi.org/10.1021/ja5105987.
ieee: P. Schanda et al., “Atomic model of a cell-wall cross-linking enzyme
in complex with an intact bacterial peptidoglycan,” Journal of the American
Chemical Society, vol. 136, no. 51. American Chemical Society, pp. 17852–17860,
2014.
ista: Schanda P, Triboulet S, Laguri C, Bougault CM, Ayala I, Callon M, Arthur M,
Simorre J-P. 2014. Atomic model of a cell-wall cross-linking enzyme in complex
with an intact bacterial peptidoglycan. Journal of the American Chemical Society.
136(51), 17852–17860.
mla: Schanda, Paul, et al. “Atomic Model of a Cell-Wall Cross-Linking Enzyme in
Complex with an Intact Bacterial Peptidoglycan.” Journal of the American Chemical
Society, vol. 136, no. 51, American Chemical Society, 2014, pp. 17852–60,
doi:10.1021/ja5105987.
short: P. Schanda, S. Triboulet, C. Laguri, C.M. Bougault, I. Ayala, M. Callon,
M. Arthur, J.-P. Simorre, Journal of the American Chemical Society 136 (2014)
17852–17860.
date_created: 2020-09-18T10:07:52Z
date_published: 2014-11-27T00:00:00Z
date_updated: 2021-01-12T08:19:24Z
day: '27'
doi: 10.1021/ja5105987
extern: '1'
intvolume: ' 136'
issue: '51'
language:
- iso: eng
month: '11'
oa_version: None
page: 17852-17860
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: Atomic model of a cell-wall cross-linking enzyme in complex with an intact
bacterial peptidoglycan
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 136
year: '2014'
...
---
_id: '8465'
abstract:
- lang: eng
text: We demonstrate that conformational exchange processes in proteins on microsecond-to-millisecond
time scales can be detected and quantified by solid-state NMR spectroscopy. We
show two independent approaches that measure the effect of conformational exchange
on transverse relaxation parameters, namely Carr–Purcell–Meiboom–Gill relaxation-dispersion
experiments and measurement of differential multiple-quantum coherence decay.
Long coherence lifetimes, as required for these experiments, are achieved by the
use of highly deuterated samples and fast magic-angle spinning. The usefulness
of the approaches is demonstrated by application to microcrystalline ubiquitin.
We detect a conformational exchange process in a region of the protein for which
dynamics have also been observed in solution. Interestingly, quantitative analysis
of the data reveals that the exchange process is more than 1 order of magnitude
slower than in solution, and this points to the impact of the crystalline environment
on free energy barriers.
article_processing_charge: No
article_type: original
author:
- first_name: Martin
full_name: Tollinger, Martin
last_name: Tollinger
- first_name: Astrid C.
full_name: Sivertsen, Astrid C.
last_name: Sivertsen
- first_name: Beat H.
full_name: Meier, Beat H.
last_name: Meier
- first_name: Matthias
full_name: Ernst, Matthias
last_name: Ernst
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: Tollinger M, Sivertsen AC, Meier BH, Ernst M, Schanda P. Site-resolved measurement
of microsecond-to-millisecond conformational-exchange processes in proteins by
solid-state NMR spectroscopy. Journal of the American Chemical Society.
2012;134(36):14800-14807. doi:10.1021/ja303591y
apa: Tollinger, M., Sivertsen, A. C., Meier, B. H., Ernst, M., & Schanda, P.
(2012). Site-resolved measurement of microsecond-to-millisecond conformational-exchange
processes in proteins by solid-state NMR spectroscopy. Journal of the American
Chemical Society. American Chemical Society. https://doi.org/10.1021/ja303591y
chicago: Tollinger, Martin, Astrid C. Sivertsen, Beat H. Meier, Matthias Ernst,
and Paul Schanda. “Site-Resolved Measurement of Microsecond-to-Millisecond Conformational-Exchange
Processes in Proteins by Solid-State NMR Spectroscopy.” Journal of the American
Chemical Society. American Chemical Society, 2012. https://doi.org/10.1021/ja303591y.
ieee: M. Tollinger, A. C. Sivertsen, B. H. Meier, M. Ernst, and P. Schanda, “Site-resolved
measurement of microsecond-to-millisecond conformational-exchange processes in
proteins by solid-state NMR spectroscopy,” Journal of the American Chemical
Society, vol. 134, no. 36. American Chemical Society, pp. 14800–14807, 2012.
ista: Tollinger M, Sivertsen AC, Meier BH, Ernst M, Schanda P. 2012. Site-resolved
measurement of microsecond-to-millisecond conformational-exchange processes in
proteins by solid-state NMR spectroscopy. Journal of the American Chemical Society.
134(36), 14800–14807.
mla: Tollinger, Martin, et al. “Site-Resolved Measurement of Microsecond-to-Millisecond
Conformational-Exchange Processes in Proteins by Solid-State NMR Spectroscopy.”
Journal of the American Chemical Society, vol. 134, no. 36, American Chemical
Society, 2012, pp. 14800–07, doi:10.1021/ja303591y.
short: M. Tollinger, A.C. Sivertsen, B.H. Meier, M. Ernst, P. Schanda, Journal of
the American Chemical Society 134 (2012) 14800–14807.
date_created: 2020-09-18T10:10:20Z
date_published: 2012-08-21T00:00:00Z
date_updated: 2021-01-12T08:19:27Z
day: '21'
doi: 10.1021/ja303591y
extern: '1'
intvolume: ' 134'
issue: '36'
language:
- iso: eng
month: '08'
oa_version: None
page: 14800-14807
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: Site-resolved measurement of microsecond-to-millisecond conformational-exchange
processes in proteins by solid-state NMR spectroscopy
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 134
year: '2012'
...
---
_id: '8466'
abstract:
- lang: eng
text: Recent advances in NMR spectroscopy and the availability of high magnetic
field strengths now offer the possibility to record real-time 3D NMR spectra of
short-lived protein states, e.g., states that become transiently populated during
protein folding. Here we present a strategy for obtaining sequential NMR assignments
as well as atom-resolved information on structural and dynamic features within
a folding intermediate of the amyloidogenic protein β2-microglobulin that has
a half-lifetime of only 20 min.
article_processing_charge: No
article_type: original
author:
- first_name: Enrico
full_name: Rennella, Enrico
last_name: Rennella
- first_name: Thomas
full_name: Cutuil, Thomas
last_name: Cutuil
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Isabel
full_name: Ayala, Isabel
last_name: Ayala
- first_name: Vincent
full_name: Forge, Vincent
last_name: Forge
- first_name: Bernhard
full_name: Brutscher, Bernhard
last_name: Brutscher
citation:
ama: Rennella E, Cutuil T, Schanda P, Ayala I, Forge V, Brutscher B. Real-time NMR
characterization of structure and dynamics in a transiently populated protein
folding intermediate. Journal of the American Chemical Society. 2012;134(19):8066-8069.
doi:10.1021/ja302598j
apa: Rennella, E., Cutuil, T., Schanda, P., Ayala, I., Forge, V., & Brutscher,
B. (2012). Real-time NMR characterization of structure and dynamics in a transiently
populated protein folding intermediate. Journal of the American Chemical Society.
American Chemical Society. https://doi.org/10.1021/ja302598j
chicago: Rennella, Enrico, Thomas Cutuil, Paul Schanda, Isabel Ayala, Vincent Forge,
and Bernhard Brutscher. “Real-Time NMR Characterization of Structure and Dynamics
in a Transiently Populated Protein Folding Intermediate.” Journal of the American
Chemical Society. American Chemical Society, 2012. https://doi.org/10.1021/ja302598j.
ieee: E. Rennella, T. Cutuil, P. Schanda, I. Ayala, V. Forge, and B. Brutscher,
“Real-time NMR characterization of structure and dynamics in a transiently populated
protein folding intermediate,” Journal of the American Chemical Society,
vol. 134, no. 19. American Chemical Society, pp. 8066–8069, 2012.
ista: Rennella E, Cutuil T, Schanda P, Ayala I, Forge V, Brutscher B. 2012. Real-time
NMR characterization of structure and dynamics in a transiently populated protein
folding intermediate. Journal of the American Chemical Society. 134(19), 8066–8069.
mla: Rennella, Enrico, et al. “Real-Time NMR Characterization of Structure and Dynamics
in a Transiently Populated Protein Folding Intermediate.” Journal of the American
Chemical Society, vol. 134, no. 19, American Chemical Society, 2012, pp. 8066–69,
doi:10.1021/ja302598j.
short: E. Rennella, T. Cutuil, P. Schanda, I. Ayala, V. Forge, B. Brutscher, Journal
of the American Chemical Society 134 (2012) 8066–8069.
date_created: 2020-09-18T10:10:28Z
date_published: 2012-05-03T00:00:00Z
date_updated: 2021-01-12T08:19:28Z
day: '03'
doi: 10.1021/ja302598j
extern: '1'
intvolume: ' 134'
issue: '19'
language:
- iso: eng
month: '05'
oa_version: None
page: 8066-8069
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: Real-time NMR characterization of structure and dynamics in a transiently populated
protein folding intermediate
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 134
year: '2012'
...
---
_id: '7308'
abstract:
- lang: eng
text: 'Carbon has been used widely as the basis of porous cathodes for nonaqueous
Li–O2 cells. However, the stability of carbon and the effect of carbon on electrolyte
decomposition in such cells are complex and depend on the hydrophobicity/hydrophilicity
of the carbon surface. Analyzing carbon cathodes, cycled in Li–O2 cells between
2 and 4 V, using acid treatment and Fenton’s reagent, and combined with differential
electrochemical mass spectrometry and FTIR, demonstrates the following: Carbon
is relatively stable below 3.5 V (vs Li/Li+) on discharge or charge, especially
so for hydrophobic carbon, but is unstable on charging above 3.5 V (in the presence
of Li2O2), oxidatively decomposing to form Li2CO3. Direct chemical reaction with
Li2O2 accounts for only a small proportion of the total carbon decomposition on
cycling. Carbon promotes electrolyte decomposition during discharge and charge
in a Li–O2 cell, giving rise to Li2CO3 and Li carboxylates (DMSO and tetraglyme
electrolytes). The Li2CO3 and Li carboxylates present at the end of discharge
and those that form on charge result in polarization on the subsequent charge.
Li2CO3 (derived from carbon and from the electrolyte) as well as the Li carboxylates
(derived from the electrolyte) decompose and form on charging. Oxidation of Li2CO3
on charging to ∼4 V is incomplete; Li2CO3 accumulates on cycling resulting in
electrode passivation and capacity fading. Hydrophilic carbon is less stable and
more catalytically active toward electrolyte decomposition than carbon with a
hydrophobic surface. If the Li–O2 cell could be charged at or below 3.5 V, then
carbon may be relatively stable, however, its ability to promote electrolyte decomposition,
presenting problems for its use in a practical Li–O2 battery. The results emphasize
that stable cycling of Li2O2 at the cathode in a Li–O2 cell depends on the synergy
between electrolyte and electrode; the stability of the electrode and the electrolyte
cannot be considered in isolation.'
article_processing_charge: No
article_type: original
author:
- first_name: Muhammed M.
full_name: Ottakam Thotiyl, Muhammed M.
last_name: Ottakam Thotiyl
- first_name: Stefan Alexander
full_name: Freunberger, Stefan Alexander
id: A8CA28E6-CE23-11E9-AD2D-EC27E6697425
last_name: Freunberger
orcid: 0000-0003-2902-5319
- first_name: Zhangquan
full_name: Peng, Zhangquan
last_name: Peng
- first_name: Peter G.
full_name: Bruce, Peter G.
last_name: Bruce
citation:
ama: Ottakam Thotiyl MM, Freunberger SA, Peng Z, Bruce PG. The carbon electrode
in nonaqueous Li–O2 cells. Journal of the American Chemical Society. 2012;135(1):494-500.
doi:10.1021/ja310258x
apa: Ottakam Thotiyl, M. M., Freunberger, S. A., Peng, Z., & Bruce, P. G. (2012).
The carbon electrode in nonaqueous Li–O2 cells. Journal of the American Chemical
Society. ACS. https://doi.org/10.1021/ja310258x
chicago: Ottakam Thotiyl, Muhammed M., Stefan Alexander Freunberger, Zhangquan Peng,
and Peter G. Bruce. “The Carbon Electrode in Nonaqueous Li–O2 Cells.” Journal
of the American Chemical Society. ACS, 2012. https://doi.org/10.1021/ja310258x.
ieee: M. M. Ottakam Thotiyl, S. A. Freunberger, Z. Peng, and P. G. Bruce, “The carbon
electrode in nonaqueous Li–O2 cells,” Journal of the American Chemical Society,
vol. 135, no. 1. ACS, pp. 494–500, 2012.
ista: Ottakam Thotiyl MM, Freunberger SA, Peng Z, Bruce PG. 2012. The carbon electrode
in nonaqueous Li–O2 cells. Journal of the American Chemical Society. 135(1), 494–500.
mla: Ottakam Thotiyl, Muhammed M., et al. “The Carbon Electrode in Nonaqueous Li–O2
Cells.” Journal of the American Chemical Society, vol. 135, no. 1, ACS,
2012, pp. 494–500, doi:10.1021/ja310258x.
short: M.M. Ottakam Thotiyl, S.A. Freunberger, Z. Peng, P.G. Bruce, Journal of the
American Chemical Society 135 (2012) 494–500.
date_created: 2020-01-15T12:18:57Z
date_published: 2012-11-28T00:00:00Z
date_updated: 2021-01-12T08:12:56Z
day: '28'
doi: 10.1021/ja310258x
extern: '1'
intvolume: ' 135'
issue: '1'
language:
- iso: eng
month: '11'
oa_version: None
page: 494-500
publication: Journal of the American Chemical Society
publication_identifier:
issn:
- 0002-7863
- 1520-5126
publication_status: published
publisher: ACS
quality_controlled: '1'
status: public
title: The carbon electrode in nonaqueous Li–O2 cells
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 135
year: '2012'
...
---
_id: '7311'
abstract:
- lang: eng
text: Stability of the electrolyte toward reduced oxygen species generated at the
cathode is a crucial challenge for the rechargeable nonaqueous Li–O2 battery.
Here, we investigate dimethylformamide as the basis of an electrolyte. Although
reactions at the O2 cathode on the first discharge–charge cycle are dominated
by reversible Li2O2 formation/decomposition, there is also electrolyte decomposition,
which increases on cycling. The products of decomposition at the cathode on discharge
are Li2O2, Li2CO3, HCO2Li, CH3CO2Li, NO, H2O, and CO2. Li2CO3 accumulates in the
electrode with cycling. The stability of dimethylformamide toward reduced oxygen
species is insufficient for its use in the rechargeable nonaqueous Li–O2 battery.
article_processing_charge: No
article_type: original
author:
- first_name: Yuhui
full_name: Chen, Yuhui
last_name: Chen
- first_name: Stefan Alexander
full_name: Freunberger, Stefan Alexander
id: A8CA28E6-CE23-11E9-AD2D-EC27E6697425
last_name: Freunberger
orcid: 0000-0003-2902-5319
- first_name: Zhangquan
full_name: Peng, Zhangquan
last_name: Peng
- first_name: Fanny
full_name: Bardé, Fanny
last_name: Bardé
- first_name: Peter G.
full_name: Bruce, Peter G.
last_name: Bruce
citation:
ama: Chen Y, Freunberger SA, Peng Z, Bardé F, Bruce PG. Li–O2 battery with a dimethylformamide
electrolyte. Journal of the American Chemical Society. 2012;134(18):7952-7957.
doi:10.1021/ja302178w
apa: Chen, Y., Freunberger, S. A., Peng, Z., Bardé, F., & Bruce, P. G. (2012).
Li–O2 battery with a dimethylformamide electrolyte. Journal of the American
Chemical Society. ACS. https://doi.org/10.1021/ja302178w
chicago: Chen, Yuhui, Stefan Alexander Freunberger, Zhangquan Peng, Fanny Bardé,
and Peter G. Bruce. “Li–O2 Battery with a Dimethylformamide Electrolyte.” Journal
of the American Chemical Society. ACS, 2012. https://doi.org/10.1021/ja302178w.
ieee: Y. Chen, S. A. Freunberger, Z. Peng, F. Bardé, and P. G. Bruce, “Li–O2 battery
with a dimethylformamide electrolyte,” Journal of the American Chemical Society,
vol. 134, no. 18. ACS, pp. 7952–7957, 2012.
ista: Chen Y, Freunberger SA, Peng Z, Bardé F, Bruce PG. 2012. Li–O2 battery with
a dimethylformamide electrolyte. Journal of the American Chemical Society. 134(18),
7952–7957.
mla: Chen, Yuhui, et al. “Li–O2 Battery with a Dimethylformamide Electrolyte.” Journal
of the American Chemical Society, vol. 134, no. 18, ACS, 2012, pp. 7952–57,
doi:10.1021/ja302178w.
short: Y. Chen, S.A. Freunberger, Z. Peng, F. Bardé, P.G. Bruce, Journal of the
American Chemical Society 134 (2012) 7952–7957.
date_created: 2020-01-15T12:19:36Z
date_published: 2012-04-19T00:00:00Z
date_updated: 2021-01-12T08:12:58Z
day: '19'
doi: 10.1021/ja302178w
extern: '1'
intvolume: ' 134'
issue: '18'
language:
- iso: eng
month: '04'
oa_version: None
page: 7952-7957
publication: Journal of the American Chemical Society
publication_identifier:
issn:
- 0002-7863
- 1520-5126
publication_status: published
publisher: ACS
quality_controlled: '1'
status: public
title: Li–O2 battery with a dimethylformamide electrolyte
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 134
year: '2012'
...
---
_id: '7316'
abstract:
- lang: eng
text: The nonaqueous rechargeable lithium–O2 battery containing an alkyl carbonate
electrolyte discharges by formation of C3H6(OCO2Li)2, Li2CO3, HCO2Li, CH3CO2Li,
CO2, and H2O at the cathode, due to electrolyte decomposition. Charging involves
oxidation of C3H6(OCO2Li)2, Li2CO3, HCO2Li, CH3CO2Li accompanied by CO2 and H2O
evolution. Mechanisms are proposed for the reactions on discharge and charge.
The different pathways for discharge and charge are consistent with the widely
observed voltage gap in Li–O2 cells. Oxidation of C3H6(OCO2Li)2 involves terminal
carbonate groups leaving behind the OC3H6O moiety that reacts to form a thick
gel on the Li anode. Li2CO3, HCO2Li, CH3CO2Li, and C3H6(OCO2Li)2 accumulate in
the cathode on cycling correlating with capacity fading and cell failure. The
latter is compounded by continuous consumption of the electrolyte on each discharge.
article_processing_charge: No
article_type: original
author:
- first_name: Stefan Alexander
full_name: Freunberger, Stefan Alexander
id: A8CA28E6-CE23-11E9-AD2D-EC27E6697425
last_name: Freunberger
orcid: 0000-0003-2902-5319
- first_name: Yuhui
full_name: Chen, Yuhui
last_name: Chen
- first_name: Zhangquan
full_name: Peng, Zhangquan
last_name: Peng
- first_name: John M.
full_name: Griffin, John M.
last_name: Griffin
- first_name: Laurence J.
full_name: Hardwick, Laurence J.
last_name: Hardwick
- first_name: Fanny
full_name: Bardé, Fanny
last_name: Bardé
- first_name: Petr
full_name: Novák, Petr
last_name: Novák
- first_name: Peter G.
full_name: Bruce, Peter G.
last_name: Bruce
citation:
ama: Freunberger SA, Chen Y, Peng Z, et al. Reactions in the rechargeable Lithium–O2
battery with alkyl carbonate electrolytes. Journal of the American Chemical
Society. 2011;133(20):8040-8047. doi:10.1021/ja2021747
apa: Freunberger, S. A., Chen, Y., Peng, Z., Griffin, J. M., Hardwick, L. J., Bardé,
F., … Bruce, P. G. (2011). Reactions in the rechargeable Lithium–O2 battery with
alkyl carbonate electrolytes. Journal of the American Chemical Society.
ACS. https://doi.org/10.1021/ja2021747
chicago: Freunberger, Stefan Alexander, Yuhui Chen, Zhangquan Peng, John M. Griffin,
Laurence J. Hardwick, Fanny Bardé, Petr Novák, and Peter G. Bruce. “Reactions
in the Rechargeable Lithium–O2 Battery with Alkyl Carbonate Electrolytes.” Journal
of the American Chemical Society. ACS, 2011. https://doi.org/10.1021/ja2021747.
ieee: S. A. Freunberger et al., “Reactions in the rechargeable Lithium–O2
battery with alkyl carbonate electrolytes,” Journal of the American Chemical
Society, vol. 133, no. 20. ACS, pp. 8040–8047, 2011.
ista: Freunberger SA, Chen Y, Peng Z, Griffin JM, Hardwick LJ, Bardé F, Novák
P, Bruce PG. 2011. Reactions in the rechargeable Lithium–O2 battery with alkyl
carbonate electrolytes. Journal of the American Chemical Society. 133(20), 8040–8047.
mla: Freunberger, Stefan Alexander, et al. “Reactions in the Rechargeable Lithium–O2
Battery with Alkyl Carbonate Electrolytes.” Journal of the American Chemical
Society, vol. 133, no. 20, ACS, 2011, pp. 8040–47, doi:10.1021/ja2021747.
short: S.A. Freunberger, Y. Chen, Z. Peng, J.M. Griffin, L.J. Hardwick, F. Bardé,
P. Novák, P.G. Bruce, Journal of the American Chemical Society 133 (2011) 8040–8047.
date_created: 2020-01-15T12:20:43Z
date_published: 2011-04-27T00:00:00Z
date_updated: 2021-01-12T08:13:00Z
day: '27'
doi: 10.1021/ja2021747
extern: '1'
intvolume: ' 133'
issue: '20'
language:
- iso: eng
month: '04'
oa_version: None
page: 8040-8047
publication: Journal of the American Chemical Society
publication_identifier:
issn:
- 0002-7863
- 1520-5126
publication_status: published
publisher: ACS
quality_controlled: '1'
status: public
title: Reactions in the rechargeable Lithium–O2 battery with alkyl carbonate electrolytes
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 133
year: '2011'
...
---
_id: '8472'
abstract:
- lang: eng
text: Characterization of protein dynamics by solid-state NMR spectroscopy requires
robust and accurate measurement protocols, which are not yet fully developed.
In this study, we investigate the backbone dynamics of microcrystalline ubiquitin
using different approaches. A rotational-echo double-resonance type (REDOR-type)
methodology allows one to accurately measure 1H−15N order parameters in highly
deuterated samples. We show that the systematic errors in the REDOR experiment
are as low as 1% or even less, giving access to accurate data for the amplitudes
of backbone mobility. Combining such dipolar-coupling-derived order parameters
with autocorrelated and cross-correlated 15N relaxation rates, we are able to
quantitate amplitudes and correlation times of backbone dynamics on picosecond
and nanosecond time scales in a residue-resolved manner. While the mobility on
picosecond time scales appears to have rather uniform amplitude throughout the
protein, we unambiguously identify and quantitate nanosecond mobility with order
parameters S2 as low as 0.8 in some regions of the protein, where nanosecond dynamics
has also been revealed in solution state. The methodology used here, a combination
of accurate dipolar-coupling measurements and different relaxation parameters,
yields details about dynamics on different time scales and can be applied to solid
protein samples such as amyloid fibrils or membrane proteins.
article_processing_charge: No
article_type: original
author:
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Beat H.
full_name: Meier, Beat H.
last_name: Meier
- first_name: Matthias
full_name: Ernst, Matthias
last_name: Ernst
citation:
ama: Schanda P, Meier BH, Ernst M. Quantitative analysis of protein backbone dynamics
in microcrystalline ubiquitin by solid-state NMR spectroscopy. Journal of the
American Chemical Society. 2010;132(45):15957-15967. doi:10.1021/ja100726a
apa: Schanda, P., Meier, B. H., & Ernst, M. (2010). Quantitative analysis of
protein backbone dynamics in microcrystalline ubiquitin by solid-state NMR spectroscopy.
Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/ja100726a
chicago: Schanda, Paul, Beat H. Meier, and Matthias Ernst. “Quantitative Analysis
of Protein Backbone Dynamics in Microcrystalline Ubiquitin by Solid-State NMR
Spectroscopy.” Journal of the American Chemical Society. American Chemical
Society, 2010. https://doi.org/10.1021/ja100726a.
ieee: P. Schanda, B. H. Meier, and M. Ernst, “Quantitative analysis of protein backbone
dynamics in microcrystalline ubiquitin by solid-state NMR spectroscopy,” Journal
of the American Chemical Society, vol. 132, no. 45. American Chemical Society,
pp. 15957–15967, 2010.
ista: Schanda P, Meier BH, Ernst M. 2010. Quantitative analysis of protein backbone
dynamics in microcrystalline ubiquitin by solid-state NMR spectroscopy. Journal
of the American Chemical Society. 132(45), 15957–15967.
mla: Schanda, Paul, et al. “Quantitative Analysis of Protein Backbone Dynamics in
Microcrystalline Ubiquitin by Solid-State NMR Spectroscopy.” Journal of the
American Chemical Society, vol. 132, no. 45, American Chemical Society, 2010,
pp. 15957–67, doi:10.1021/ja100726a.
short: P. Schanda, B.H. Meier, M. Ernst, Journal of the American Chemical Society
132 (2010) 15957–15967.
date_created: 2020-09-18T10:11:13Z
date_published: 2010-10-26T00:00:00Z
date_updated: 2021-01-12T08:19:30Z
day: '26'
doi: 10.1021/ja100726a
extern: '1'
intvolume: ' 132'
issue: '45'
language:
- iso: eng
month: '10'
oa_version: None
page: 15957-15967
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: Quantitative analysis of protein backbone dynamics in microcrystalline ubiquitin
by solid-state NMR spectroscopy
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 132
year: '2010'
...
---
_id: '8476'
abstract:
- lang: eng
text: Atomic-resolution information on the structure and dynamics of nucleic acids
is essential for a better understanding of the mechanistic basis of many cellular
processes. NMR spectroscopy is a powerful method for studying the structure and
dynamics of nucleic acids; however, solution NMR studies are currently limited
to relatively small nucleic acids at high concentrations. Thus, technological
and methodological improvements that increase the experimental sensitivity and
spectral resolution of NMR spectroscopy are required for studies of larger nucleic
acids or protein−nucleic acid complexes. Here we introduce a series of imino-proton-detected
NMR experiments that yield an over 2-fold increase in sensitivity compared to
conventional pulse schemes. These methods can be applied to the detection of base
pair interactions, RNA−ligand titration experiments, measurement of residual dipolar
15N−1H couplings, and direct measurements of conformational transitions. These
NMR experiments employ longitudinal spin relaxation enhancement techniques that
have proven useful in protein NMR spectroscopy. The performance of these new experiments
is demonstrated for a 10 kDa TAR-TAR*GA RNA kissing complex and a 26 kDa tRNA.
article_processing_charge: No
article_type: original
author:
- first_name: Jonathan
full_name: Farjon, Jonathan
last_name: Farjon
- first_name: Jérôme
full_name: Boisbouvier, Jérôme
last_name: Boisbouvier
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Arthur
full_name: Pardi, Arthur
last_name: Pardi
- first_name: Jean-Pierre
full_name: Simorre, Jean-Pierre
last_name: Simorre
- first_name: Bernhard
full_name: Brutscher, Bernhard
last_name: Brutscher
citation:
ama: Farjon J, Boisbouvier J, Schanda P, Pardi A, Simorre J-P, Brutscher B. Longitudinal-relaxation-enhanced
NMR experiments for the study of nucleic acids in solution. Journal of the
American Chemical Society. 2009;131(24):8571-8577. doi:10.1021/ja901633y
apa: Farjon, J., Boisbouvier, J., Schanda, P., Pardi, A., Simorre, J.-P., &
Brutscher, B. (2009). Longitudinal-relaxation-enhanced NMR experiments for the
study of nucleic acids in solution. Journal of the American Chemical Society.
American Chemical Society. https://doi.org/10.1021/ja901633y
chicago: Farjon, Jonathan, Jérôme Boisbouvier, Paul Schanda, Arthur Pardi, Jean-Pierre
Simorre, and Bernhard Brutscher. “Longitudinal-Relaxation-Enhanced NMR Experiments
for the Study of Nucleic Acids in Solution.” Journal of the American Chemical
Society. American Chemical Society, 2009. https://doi.org/10.1021/ja901633y.
ieee: J. Farjon, J. Boisbouvier, P. Schanda, A. Pardi, J.-P. Simorre, and B. Brutscher,
“Longitudinal-relaxation-enhanced NMR experiments for the study of nucleic acids
in solution,” Journal of the American Chemical Society, vol. 131, no. 24.
American Chemical Society, pp. 8571–8577, 2009.
ista: Farjon J, Boisbouvier J, Schanda P, Pardi A, Simorre J-P, Brutscher B. 2009.
Longitudinal-relaxation-enhanced NMR experiments for the study of nucleic acids
in solution. Journal of the American Chemical Society. 131(24), 8571–8577.
mla: Farjon, Jonathan, et al. “Longitudinal-Relaxation-Enhanced NMR Experiments
for the Study of Nucleic Acids in Solution.” Journal of the American Chemical
Society, vol. 131, no. 24, American Chemical Society, 2009, pp. 8571–77, doi:10.1021/ja901633y.
short: J. Farjon, J. Boisbouvier, P. Schanda, A. Pardi, J.-P. Simorre, B. Brutscher,
Journal of the American Chemical Society 131 (2009) 8571–8577.
date_created: 2020-09-18T10:11:49Z
date_published: 2009-06-01T00:00:00Z
date_updated: 2021-01-12T08:19:32Z
day: '01'
doi: 10.1021/ja901633y
extern: '1'
intvolume: ' 131'
issue: '24'
language:
- iso: eng
month: '06'
oa_version: None
page: 8571-8577
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: Longitudinal-relaxation-enhanced NMR experiments for the study of nucleic acids
in solution
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 131
year: '2009'
...
---
_id: '8477'
abstract:
- lang: eng
text: An optimized NMR experiment that combines the advantages of methyl-TROSY and
SOFAST-HMQC has been developed. It allows the recording of high quality methyl
1H−13C correlation spectra of protein assemblies of several hundreds of kDa in
a few seconds. The SOFAST-methyl-TROSY-based experiment offers completely new
opportunities for the study of structural and dynamic changes occurring in molecular
nanomachines while they perform their biological function in vitro.
article_processing_charge: No
article_type: original
author:
- first_name: Carlos
full_name: Amero, Carlos
last_name: Amero
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: M. Asunción
full_name: Durá, M. Asunción
last_name: Durá
- first_name: Isabel
full_name: Ayala, Isabel
last_name: Ayala
- first_name: Dominique
full_name: Marion, Dominique
last_name: Marion
- first_name: Bruno
full_name: Franzetti, Bruno
last_name: Franzetti
- first_name: Bernhard
full_name: Brutscher, Bernhard
last_name: Brutscher
- first_name: Jérôme
full_name: Boisbouvier, Jérôme
last_name: Boisbouvier
citation:
ama: Amero C, Schanda P, Durá MA, et al. Fast two-dimensional NMR spectroscopy
of high molecular weight protein assemblies. Journal of the American Chemical
Society. 2009;131(10):3448-3449. doi:10.1021/ja809880p
apa: Amero, C., Schanda, P., Durá, M. A., Ayala, I., Marion, D., Franzetti, B.,
… Boisbouvier, J. (2009). Fast two-dimensional NMR spectroscopy of high molecular
weight protein assemblies. Journal of the American Chemical Society. American
Chemical Society. https://doi.org/10.1021/ja809880p
chicago: Amero, Carlos, Paul Schanda, M. Asunción Durá, Isabel Ayala, Dominique
Marion, Bruno Franzetti, Bernhard Brutscher, and Jérôme Boisbouvier. “Fast Two-Dimensional
NMR Spectroscopy of High Molecular Weight Protein Assemblies.” Journal of the
American Chemical Society. American Chemical Society, 2009. https://doi.org/10.1021/ja809880p.
ieee: C. Amero et al., “Fast two-dimensional NMR spectroscopy of high molecular
weight protein assemblies,” Journal of the American Chemical Society, vol.
131, no. 10. American Chemical Society, pp. 3448–3449, 2009.
ista: Amero C, Schanda P, Durá MA, Ayala I, Marion D, Franzetti B, Brutscher B,
Boisbouvier J. 2009. Fast two-dimensional NMR spectroscopy of high molecular weight
protein assemblies. Journal of the American Chemical Society. 131(10), 3448–3449.
mla: Amero, Carlos, et al. “Fast Two-Dimensional NMR Spectroscopy of High Molecular
Weight Protein Assemblies.” Journal of the American Chemical Society, vol.
131, no. 10, American Chemical Society, 2009, pp. 3448–49, doi:10.1021/ja809880p.
short: C. Amero, P. Schanda, M.A. Durá, I. Ayala, D. Marion, B. Franzetti, B. Brutscher,
J. Boisbouvier, Journal of the American Chemical Society 131 (2009) 3448–3449.
date_created: 2020-09-18T10:12:01Z
date_published: 2009-02-25T00:00:00Z
date_updated: 2021-01-12T08:19:32Z
day: '25'
doi: 10.1021/ja809880p
extern: '1'
intvolume: ' 131'
issue: '10'
language:
- iso: eng
month: '02'
oa_version: None
page: 3448-3449
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: Fast two-dimensional NMR spectroscopy of high molecular weight protein assemblies
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 131
year: '2009'
...
---
_id: '8478'
abstract:
- lang: eng
text: Allosteric regulation is an effective mechanism of control in biological processes.
In allosteric proteins a signal originating at one site in the molecule is communicated
through the protein structure to trigger a specific response at a remote site.
Using NMR relaxation dispersion techniques we directly observe the dynamic process
through which the KIX domain of CREB binding protein communicates allosteric information
between binding sites. KIX mediates cooperativity between pairs of transcription
factors through binding to two distinct interaction surfaces in an allosteric
manner. We show that binding the activation domain of the mixed lineage leukemia
(MLL) transcription factor to KIX induces a redistribution of the relative populations
of KIX conformations toward a high-energy state in which the allosterically activated
second binding site is already preformed, consistent with the Monod−Wyman−Changeux
(WMC) model of allostery. The structural rearrangement process that links the
two conformers and by which allosteric information is communicated occurs with
a time constant of 3 ms at 27 °C. Our dynamic NMR data reveal that an evolutionarily
conserved network of hydrophobic amino acids constitutes the pathway through which
information is transmitted.
article_processing_charge: No
article_type: original
author:
- first_name: Sven
full_name: Brüschweiler, Sven
last_name: Brüschweiler
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Karin
full_name: Kloiber, Karin
last_name: Kloiber
- first_name: Bernhard
full_name: Brutscher, Bernhard
last_name: Brutscher
- first_name: Georg
full_name: Kontaxis, Georg
last_name: Kontaxis
- first_name: Robert
full_name: Konrat, Robert
last_name: Konrat
- first_name: Martin
full_name: Tollinger, Martin
last_name: Tollinger
citation:
ama: Brüschweiler S, Schanda P, Kloiber K, et al. Direct observation of the dynamic
process underlying allosteric signal transmission. Journal of the American
Chemical Society. 2009;131(8):3063-3068. doi:10.1021/ja809947w
apa: Brüschweiler, S., Schanda, P., Kloiber, K., Brutscher, B., Kontaxis, G., Konrat,
R., & Tollinger, M. (2009). Direct observation of the dynamic process underlying
allosteric signal transmission. Journal of the American Chemical Society.
American Chemical Society. https://doi.org/10.1021/ja809947w
chicago: Brüschweiler, Sven, Paul Schanda, Karin Kloiber, Bernhard Brutscher, Georg
Kontaxis, Robert Konrat, and Martin Tollinger. “Direct Observation of the Dynamic
Process Underlying Allosteric Signal Transmission.” Journal of the American
Chemical Society. American Chemical Society, 2009. https://doi.org/10.1021/ja809947w.
ieee: S. Brüschweiler et al., “Direct observation of the dynamic process
underlying allosteric signal transmission,” Journal of the American Chemical
Society, vol. 131, no. 8. American Chemical Society, pp. 3063–3068, 2009.
ista: Brüschweiler S, Schanda P, Kloiber K, Brutscher B, Kontaxis G, Konrat R,
Tollinger M. 2009. Direct observation of the dynamic process underlying allosteric
signal transmission. Journal of the American Chemical Society. 131(8), 3063–3068.
mla: Brüschweiler, Sven, et al. “Direct Observation of the Dynamic Process Underlying
Allosteric Signal Transmission.” Journal of the American Chemical Society,
vol. 131, no. 8, American Chemical Society, 2009, pp. 3063–68, doi:10.1021/ja809947w.
short: S. Brüschweiler, P. Schanda, K. Kloiber, B. Brutscher, G. Kontaxis, R. Konrat,
M. Tollinger, Journal of the American Chemical Society 131 (2009) 3063–3068.
date_created: 2020-09-18T10:12:14Z
date_published: 2009-02-09T00:00:00Z
date_updated: 2021-01-12T08:19:33Z
day: '09'
doi: 10.1021/ja809947w
extern: '1'
intvolume: ' 131'
issue: '8'
language:
- iso: eng
month: '02'
oa_version: None
page: 3063-3068
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: Direct observation of the dynamic process underlying allosteric signal transmission
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 131
year: '2009'
...
---
_id: '8486'
abstract:
- lang: eng
text: A technique is described that allows reducing acquisition times of multidimensional
NMR experiments by extensive spectral folding. The method is simple and has many
interesting applications for NMR studies of molecular structure, dynamics, and
kinetics.
article_processing_charge: No
article_type: original
author:
- first_name: Ewen
full_name: Lescop, Ewen
last_name: Lescop
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Rodolfo
full_name: Rasia, Rodolfo
last_name: Rasia
- first_name: Bernhard
full_name: Brutscher, Bernhard
last_name: Brutscher
citation:
ama: Lescop E, Schanda P, Rasia R, Brutscher B. Automated spectral compression for
fast multidimensional NMR and increased time resolution in real-time NMR spectroscopy.
Journal of the American Chemical Society. 2007;129(10):2756-2757. doi:10.1021/ja068949u
apa: Lescop, E., Schanda, P., Rasia, R., & Brutscher, B. (2007). Automated spectral
compression for fast multidimensional NMR and increased time resolution in real-time
NMR spectroscopy. Journal of the American Chemical Society. American Chemical
Society. https://doi.org/10.1021/ja068949u
chicago: Lescop, Ewen, Paul Schanda, Rodolfo Rasia, and Bernhard Brutscher. “Automated
Spectral Compression for Fast Multidimensional NMR and Increased Time Resolution
in Real-Time NMR Spectroscopy.” Journal of the American Chemical Society.
American Chemical Society, 2007. https://doi.org/10.1021/ja068949u.
ieee: E. Lescop, P. Schanda, R. Rasia, and B. Brutscher, “Automated spectral compression
for fast multidimensional NMR and increased time resolution in real-time NMR spectroscopy,”
Journal of the American Chemical Society, vol. 129, no. 10. American Chemical
Society, pp. 2756–2757, 2007.
ista: Lescop E, Schanda P, Rasia R, Brutscher B. 2007. Automated spectral compression
for fast multidimensional NMR and increased time resolution in real-time NMR spectroscopy.
Journal of the American Chemical Society. 129(10), 2756–2757.
mla: Lescop, Ewen, et al. “Automated Spectral Compression for Fast Multidimensional
NMR and Increased Time Resolution in Real-Time NMR Spectroscopy.” Journal of
the American Chemical Society, vol. 129, no. 10, American Chemical Society,
2007, pp. 2756–57, doi:10.1021/ja068949u.
short: E. Lescop, P. Schanda, R. Rasia, B. Brutscher, Journal of the American Chemical
Society 129 (2007) 2756–2757.
date_created: 2020-09-18T10:13:21Z
date_published: 2007-02-17T00:00:00Z
date_updated: 2021-01-12T08:19:36Z
day: '17'
doi: 10.1021/ja068949u
extern: '1'
intvolume: ' 129'
issue: '10'
keyword:
- Colloid and Surface Chemistry
- Biochemistry
- General Chemistry
- Catalysis
language:
- iso: eng
month: '02'
oa_version: None
page: 2756-2757
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: Automated spectral compression for fast multidimensional NMR and increased
time resolution in real-time NMR spectroscopy
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 129
year: '2007'
...
---
_id: '8487'
abstract:
- lang: eng
text: Following unidirectional biophysical events such as the folding of proteins
or the equilibration of binding interactions, requires experimental methods that
yield information at both atomic-level resolution and at high repetition rates.
Toward this end a number of different approaches enabling the rapid acquisition
of 2D NMR spectra have been recently introduced, including spatially encoded “ultrafast”
2D NMR spectroscopy and SOFAST HMQC NMR. Whereas the former accelerates acquisitions
by reducing the number of scans that are necessary for completing arbitrary 2D
NMR experiments, the latter operates by reducing the delay between consecutive
scans while preserving sensitivity. Given the complementarities between these
two approaches it seems natural to combine them into a single tool, enabling the
acquisition of full 2D protein NMR spectra at high repetition rates. We demonstrate
here this capability with the introduction of “ultraSOFAST” HMQC NMR, a spatially
encoded and relaxation-optimized approach that can provide 2D protein correlation
spectra at ∼1 s repetition rates for samples in the ∼2 mM concentration range.
The principles, relative advantages, and current limitations of this new approach
are discussed, and its application is exemplified with a study of the fast hydrogen−deuterium
exchange characterizing amide sites in Ubiquitin.
article_processing_charge: No
article_type: original
author:
- first_name: Maayan
full_name: Gal, Maayan
last_name: Gal
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Bernhard
full_name: Brutscher, Bernhard
last_name: Brutscher
- first_name: Lucio
full_name: Frydman, Lucio
last_name: Frydman
citation:
ama: Gal M, Schanda P, Brutscher B, Frydman L. UltraSOFAST HMQC NMR and the repetitive
acquisition of 2D protein spectra at Hz rates. Journal of the American Chemical
Society. 2007;129(5):1372-1377. doi:10.1021/ja066915g
apa: Gal, M., Schanda, P., Brutscher, B., & Frydman, L. (2007). UltraSOFAST
HMQC NMR and the repetitive acquisition of 2D protein spectra at Hz rates. Journal
of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/ja066915g
chicago: Gal, Maayan, Paul Schanda, Bernhard Brutscher, and Lucio Frydman. “UltraSOFAST
HMQC NMR and the Repetitive Acquisition of 2D Protein Spectra at Hz Rates.” Journal
of the American Chemical Society. American Chemical Society, 2007. https://doi.org/10.1021/ja066915g.
ieee: M. Gal, P. Schanda, B. Brutscher, and L. Frydman, “UltraSOFAST HMQC NMR and
the repetitive acquisition of 2D protein spectra at Hz rates,” Journal of the
American Chemical Society, vol. 129, no. 5. American Chemical Society, pp.
1372–1377, 2007.
ista: Gal M, Schanda P, Brutscher B, Frydman L. 2007. UltraSOFAST HMQC NMR and the
repetitive acquisition of 2D protein spectra at Hz rates. Journal of the American
Chemical Society. 129(5), 1372–1377.
mla: Gal, Maayan, et al. “UltraSOFAST HMQC NMR and the Repetitive Acquisition of
2D Protein Spectra at Hz Rates.” Journal of the American Chemical Society,
vol. 129, no. 5, American Chemical Society, 2007, pp. 1372–77, doi:10.1021/ja066915g.
short: M. Gal, P. Schanda, B. Brutscher, L. Frydman, Journal of the American Chemical
Society 129 (2007) 1372–1377.
date_created: 2020-09-18T10:13:27Z
date_published: 2007-01-10T00:00:00Z
date_updated: 2021-01-12T08:19:37Z
day: '10'
doi: 10.1021/ja066915g
extern: '1'
intvolume: ' 129'
issue: '5'
keyword:
- Colloid and Surface Chemistry
- Biochemistry
- General Chemistry
- Catalysis
language:
- iso: eng
month: '01'
oa_version: None
page: 1372-1377
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: UltraSOFAST HMQC NMR and the repetitive acquisition of 2D protein spectra at
Hz rates
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 129
year: '2007'
...
---
_id: '8488'
abstract:
- lang: eng
text: We demonstrate for different protein samples that three-dimensional HNCO and
HNCA correlation spectra may be recorded in a few minutes acquisition time using
the band-selective excitation short-transient sequences presented here. This opens
new perspectives for the NMR structural investigation of unstable protein samples
and real-time site-resolved studies of protein kinetics.
article_processing_charge: No
article_type: original
author:
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Hélène
full_name: Van Melckebeke, Hélène
last_name: Van Melckebeke
- first_name: Bernhard
full_name: Brutscher, Bernhard
last_name: Brutscher
citation:
ama: Schanda P, Van Melckebeke H, Brutscher B. Speeding up three-dimensional protein
NMR experiments to a few minutes. Journal of the American Chemical Society.
2006;128(28):9042-9043. doi:10.1021/ja062025p
apa: Schanda, P., Van Melckebeke, H., & Brutscher, B. (2006). Speeding up three-dimensional
protein NMR experiments to a few minutes. Journal of the American Chemical
Society. American Chemical Society. https://doi.org/10.1021/ja062025p
chicago: Schanda, Paul, Hélène Van Melckebeke, and Bernhard Brutscher. “Speeding
up Three-Dimensional Protein NMR Experiments to a Few Minutes.” Journal of
the American Chemical Society. American Chemical Society, 2006. https://doi.org/10.1021/ja062025p.
ieee: P. Schanda, H. Van Melckebeke, and B. Brutscher, “Speeding up three-dimensional
protein NMR experiments to a few minutes,” Journal of the American Chemical
Society, vol. 128, no. 28. American Chemical Society, pp. 9042–9043, 2006.
ista: Schanda P, Van Melckebeke H, Brutscher B. 2006. Speeding up three-dimensional
protein NMR experiments to a few minutes. Journal of the American Chemical Society.
128(28), 9042–9043.
mla: Schanda, Paul, et al. “Speeding up Three-Dimensional Protein NMR Experiments
to a Few Minutes.” Journal of the American Chemical Society, vol. 128,
no. 28, American Chemical Society, 2006, pp. 9042–43, doi:10.1021/ja062025p.
short: P. Schanda, H. Van Melckebeke, B. Brutscher, Journal of the American Chemical
Society 128 (2006) 9042–9043.
date_created: 2020-09-18T10:13:36Z
date_published: 2006-06-21T00:00:00Z
date_updated: 2021-01-12T08:19:37Z
day: '21'
doi: 10.1021/ja062025p
extern: '1'
intvolume: ' 128'
issue: '28'
keyword:
- Colloid and Surface Chemistry
- Biochemistry
- General Chemistry
- Catalysis
language:
- iso: eng
month: '06'
oa_version: None
page: 9042-9043
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: Speeding up three-dimensional protein NMR experiments to a few minutes
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 128
year: '2006'
...
---
_id: '8492'
abstract:
- lang: eng
text: We demonstrate for different protein samples that 2D 1H−15N correlation NMR
spectra can be recorded in a few seconds of acquisition time using a new band-selective
optimized flip-angle short-transient heteronuclear multiple quantum coherence
experiment. This has enabled us to measure fast hydrogen−deuterium exchange rate
constants along the backbone of a small globular protein fragment by real-time
2D NMR.
article_processing_charge: No
article_type: original
author:
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Bernhard
full_name: Brutscher, Bernhard
last_name: Brutscher
citation:
ama: Schanda P, Brutscher B. Very fast two-dimensional NMR spectroscopy for real-time
investigation of dynamic events in proteins on the time scale of seconds. Journal
of the American Chemical Society. 2005;127(22):8014-8015. doi:10.1021/ja051306e
apa: Schanda, P., & Brutscher, B. (2005). Very fast two-dimensional NMR spectroscopy
for real-time investigation of dynamic events in proteins on the time scale of
seconds. Journal of the American Chemical Society. American Chemical Society.
https://doi.org/10.1021/ja051306e
chicago: Schanda, Paul, and Bernhard Brutscher. “Very Fast Two-Dimensional NMR Spectroscopy
for Real-Time Investigation of Dynamic Events in Proteins on the Time Scale of
Seconds.” Journal of the American Chemical Society. American Chemical Society,
2005. https://doi.org/10.1021/ja051306e.
ieee: P. Schanda and B. Brutscher, “Very fast two-dimensional NMR spectroscopy for
real-time investigation of dynamic events in proteins on the time scale of seconds,”
Journal of the American Chemical Society, vol. 127, no. 22. American Chemical
Society, pp. 8014–8015, 2005.
ista: Schanda P, Brutscher B. 2005. Very fast two-dimensional NMR spectroscopy for
real-time investigation of dynamic events in proteins on the time scale of seconds.
Journal of the American Chemical Society. 127(22), 8014–8015.
mla: Schanda, Paul, and Bernhard Brutscher. “Very Fast Two-Dimensional NMR Spectroscopy
for Real-Time Investigation of Dynamic Events in Proteins on the Time Scale of
Seconds.” Journal of the American Chemical Society, vol. 127, no. 22, American
Chemical Society, 2005, pp. 8014–15, doi:10.1021/ja051306e.
short: P. Schanda, B. Brutscher, Journal of the American Chemical Society 127 (2005)
8014–8015.
date_created: 2020-09-18T10:14:05Z
date_published: 2005-05-14T00:00:00Z
date_updated: 2021-01-12T08:19:39Z
day: '14'
doi: 10.1021/ja051306e
extern: '1'
intvolume: ' 127'
issue: '22'
keyword:
- Colloid and Surface Chemistry
- Biochemistry
- General Chemistry
- Catalysis
language:
- iso: eng
month: '05'
oa_version: None
page: 8014-8015
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: Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic
events in proteins on the time scale of seconds
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 127
year: '2005'
...