---
_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: '13407'
abstract:
- lang: eng
text: We show that diamagnetic particles can be remotely manipulated by a magnet
by the reversible adsorption of dual-responsive, light-switchable/superparamagnetic
nanoparticles down to their surface. Adsorption occurs upon exposure to UV light,
and can be reversed thermally or by ambient light. The dynamic self-assembly of
thin films of the dual-responsive nanoparticles induces attractive interactions
between diamagnetic particles. We demonstrate that catalytic amounts of the dual-responsive
nanoparticles are sufficient to magnetically guide and deliver the diamagnetic
particles to desired locations, where they can then be released by disassembling
the dynamic layers of superparamagnetic nanoparticles with visible light.
article_processing_charge: No
article_type: original
author:
- first_name: Olga
full_name: Chovnik, Olga
last_name: Chovnik
- first_name: Renata
full_name: Balgley, Renata
last_name: Balgley
- first_name: Joel R.
full_name: Goldman, Joel R.
last_name: Goldman
- first_name: Rafal
full_name: Klajn, Rafal
id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b
last_name: Klajn
citation:
ama: Chovnik O, Balgley R, Goldman JR, Klajn R. Dynamically self-assembling carriers
enable guiding of diamagnetic particles by weak magnets. Journal of the American
Chemical Society. 2012;134(48):19564-19567. doi:10.1021/ja309633v
apa: Chovnik, O., Balgley, R., Goldman, J. R., & Klajn, R. (2012). Dynamically
self-assembling carriers enable guiding of diamagnetic particles by weak magnets.
Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/ja309633v
chicago: Chovnik, Olga, Renata Balgley, Joel R. Goldman, and Rafal Klajn. “Dynamically
Self-Assembling Carriers Enable Guiding of Diamagnetic Particles by Weak Magnets.”
Journal of the American Chemical Society. American Chemical Society, 2012.
https://doi.org/10.1021/ja309633v.
ieee: O. Chovnik, R. Balgley, J. R. Goldman, and R. Klajn, “Dynamically self-assembling
carriers enable guiding of diamagnetic particles by weak magnets,” Journal
of the American Chemical Society, vol. 134, no. 48. American Chemical Society,
pp. 19564–19567, 2012.
ista: Chovnik O, Balgley R, Goldman JR, Klajn R. 2012. Dynamically self-assembling
carriers enable guiding of diamagnetic particles by weak magnets. Journal of the
American Chemical Society. 134(48), 19564–19567.
mla: Chovnik, Olga, et al. “Dynamically Self-Assembling Carriers Enable Guiding
of Diamagnetic Particles by Weak Magnets.” Journal of the American Chemical
Society, vol. 134, no. 48, American Chemical Society, 2012, pp. 19564–67,
doi:10.1021/ja309633v.
short: O. Chovnik, R. Balgley, J.R. Goldman, R. Klajn, Journal of the American Chemical
Society 134 (2012) 19564–19567.
date_created: 2023-08-01T09:47:42Z
date_published: 2012-11-26T00:00:00Z
date_updated: 2023-08-08T07:51:10Z
day: '26'
doi: 10.1021/ja309633v
extern: '1'
external_id:
pmid:
- '23181449'
intvolume: ' 134'
issue: '48'
keyword:
- Colloid and Surface Chemistry
- Biochemistry
- General Chemistry
- Catalysis
language:
- iso: eng
month: '11'
oa_version: Published Version
page: 19564-19567
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: Dynamically self-assembling carriers enable guiding of diamagnetic particles
by weak magnets
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: '13410'
abstract:
- lang: eng
text: A range (Au, Pt, Pd) of metal nanoparticles (MNPs) has been prepared and functionalized
with (a) redox-active stalks containing tetrathiafulvalene (TTF) units, (b) [2]pseudorotaxanes
formed between these stalks and cyclobis(paraquat-p-phenylene) (CBPQT4+) rings,
and (c) bistable [2]rotaxane molecules where the dumbbell component contains a
1,5-dioxynaphthalene (DNP) unit, as well as a TTF unit, encircled by a CBPQT4+
ring. It transpires that the molecules present in (a) and (c) and the supermolecules
described in (b) retain their switching characteristics, previously observed in
solution, when they are immobilized onto MNPs. Moreover, their oxidation potentials
depend on the fraction, χ, of the molecules or supermolecules on the surface of
the nanoparticles. A variation in χ affects the oxidation potentials of the TTF
units to the extent that switching can be subjected to fine tuning as a result.
Specifically, increasing χ results in positive shifts (i) in the oxidation potentials
of the TTF unit in (a)−(c) and (ii) the reduction potentials of the CBPQT4+ rings
in (c). These shifts can be attributed to an increase in the electrostatic potential
surrounding the MNPs. Both the magnitude and the direction of these shifts are
reproduced by a model, based on the Poisson−Boltzmann equation coupled with charge-regulating
boundary conditions. Furthermore, the kinetics of relaxation from the metastable
state coconformation (MSCC) to the ground-state coconformation (GSCC) of the bistable
[2]rotaxane molecules also depends on χ, as well as on the nanoparticle diameter.
Increasing either of these parameters accelerates the rate of relaxation from
the MSCC to the GSCC. This rate is a function of (i) the activation energy for
the relaxation process associated with the bistable [2]rotaxane molecules in solution
and (ii) the electrostatic potential surrounding the MNPs. The electrostatic potential
depends on (i) the diameter of the MNPs, (ii) the amount of the bistable [2]rotaxane
molecules on the surface of the MNPs, and (iii) the equilibrium distribution of
the CBPQT4+ rings between the DNP and TTF recognition sites in the GSCC. This
electrostatic potential has also been quantified using the Poisson−Boltzmann equation,
leading to faithful estimates of the rate constants.
article_processing_charge: No
article_type: original
author:
- first_name: Ali
full_name: Coskun, Ali
last_name: Coskun
- first_name: Paul J.
full_name: Wesson, Paul J.
last_name: Wesson
- first_name: Rafal
full_name: Klajn, Rafal
id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b
last_name: Klajn
- first_name: Ali
full_name: Trabolsi, Ali
last_name: Trabolsi
- first_name: Lei
full_name: Fang, Lei
last_name: Fang
- first_name: Mark A.
full_name: Olson, Mark A.
last_name: Olson
- first_name: Sanjeev K.
full_name: Dey, Sanjeev K.
last_name: Dey
- first_name: Bartosz A.
full_name: Grzybowski, Bartosz A.
last_name: Grzybowski
- first_name: J. Fraser
full_name: Stoddart, J. Fraser
last_name: Stoddart
citation:
ama: 'Coskun A, Wesson PJ, Klajn R, et al. Molecular-mechanical switching at the
nanoparticle−solvent interface: Practice and theory. Journal of the American
Chemical Society. 2010;132(12):4310-4320. doi:10.1021/ja9102327'
apa: 'Coskun, A., Wesson, P. J., Klajn, R., Trabolsi, A., Fang, L., Olson, M. A.,
… Stoddart, J. F. (2010). Molecular-mechanical switching at the nanoparticle−solvent
interface: Practice and theory. Journal of the American Chemical Society.
American Chemical Society. https://doi.org/10.1021/ja9102327'
chicago: 'Coskun, Ali, Paul J. Wesson, Rafal Klajn, Ali Trabolsi, Lei Fang, Mark
A. Olson, Sanjeev K. Dey, Bartosz A. Grzybowski, and J. Fraser Stoddart. “Molecular-Mechanical
Switching at the Nanoparticle−solvent Interface: Practice and Theory.” Journal
of the American Chemical Society. American Chemical Society, 2010. https://doi.org/10.1021/ja9102327.'
ieee: 'A. Coskun et al., “Molecular-mechanical switching at the nanoparticle−solvent
interface: Practice and theory,” Journal of the American Chemical Society,
vol. 132, no. 12. American Chemical Society, pp. 4310–4320, 2010.'
ista: 'Coskun A, Wesson PJ, Klajn R, Trabolsi A, Fang L, Olson MA, Dey SK, Grzybowski
BA, Stoddart JF. 2010. Molecular-mechanical switching at the nanoparticle−solvent
interface: Practice and theory. Journal of the American Chemical Society. 132(12),
4310–4320.'
mla: 'Coskun, Ali, et al. “Molecular-Mechanical Switching at the Nanoparticle−solvent
Interface: Practice and Theory.” Journal of the American Chemical Society,
vol. 132, no. 12, American Chemical Society, 2010, pp. 4310–20, doi:10.1021/ja9102327.'
short: A. Coskun, P.J. Wesson, R. Klajn, A. Trabolsi, L. Fang, M.A. Olson, S.K.
Dey, B.A. Grzybowski, J.F. Stoddart, Journal of the American Chemical Society
132 (2010) 4310–4320.
date_created: 2023-08-01T09:48:27Z
date_published: 2010-03-31T00:00:00Z
date_updated: 2023-08-08T08:00:31Z
day: '31'
doi: 10.1021/ja9102327
extern: '1'
external_id:
pmid:
- '20218598'
intvolume: ' 132'
issue: '12'
keyword:
- Colloid and Surface Chemistry
- Biochemistry
- General Chemistry
- Catalysis
language:
- iso: eng
month: '03'
oa_version: None
page: 4310-4320
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: 'Molecular-mechanical switching at the nanoparticle−solvent interface: Practice
and theory'
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: '13420'
abstract:
- lang: eng
text: Weakly protected metal nanoparticles (MNPs) are used as precursors for the
preparation of catenane- and pseudorotaxane-decorated NPs of various compositions
(gold, palladium, platinum). When attached to the surface of MNPs, the molecular
switches retain their switching abilities. The redox potentials of these switches
depend on and can be regulated by the composition of the mixed self-assembled
monolayers covering the MNPs.
article_processing_charge: No
article_type: original
author:
- first_name: Rafal
full_name: Klajn, Rafal
id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b
last_name: Klajn
- first_name: Lei
full_name: Fang, Lei
last_name: Fang
- first_name: Ali
full_name: Coskun, Ali
last_name: Coskun
- first_name: Mark A.
full_name: Olson, Mark A.
last_name: Olson
- first_name: Paul J.
full_name: Wesson, Paul J.
last_name: Wesson
- first_name: J. Fraser
full_name: Stoddart, J. Fraser
last_name: Stoddart
- first_name: Bartosz A.
full_name: Grzybowski, Bartosz A.
last_name: Grzybowski
citation:
ama: Klajn R, Fang L, Coskun A, et al. Metal nanoparticles functionalized with molecular
and supramolecular switches. Journal of the American Chemical Society.
2009;131(12):4233-4235. doi:10.1021/ja9001585
apa: Klajn, R., Fang, L., Coskun, A., Olson, M. A., Wesson, P. J., Stoddart, J.
F., & Grzybowski, B. A. (2009). Metal nanoparticles functionalized with molecular
and supramolecular switches. Journal of the American Chemical Society.
American Chemical Society. https://doi.org/10.1021/ja9001585
chicago: Klajn, Rafal, Lei Fang, Ali Coskun, Mark A. Olson, Paul J. Wesson, J. Fraser
Stoddart, and Bartosz A. Grzybowski. “Metal Nanoparticles Functionalized with
Molecular and Supramolecular Switches.” Journal of the American Chemical Society.
American Chemical Society, 2009. https://doi.org/10.1021/ja9001585.
ieee: R. Klajn et al., “Metal nanoparticles functionalized with molecular
and supramolecular switches,” Journal of the American Chemical Society,
vol. 131, no. 12. American Chemical Society, pp. 4233–4235, 2009.
ista: Klajn R, Fang L, Coskun A, Olson MA, Wesson PJ, Stoddart JF, Grzybowski BA.
2009. Metal nanoparticles functionalized with molecular and supramolecular switches.
Journal of the American Chemical Society. 131(12), 4233–4235.
mla: Klajn, Rafal, et al. “Metal Nanoparticles Functionalized with Molecular and
Supramolecular Switches.” Journal of the American Chemical Society, vol.
131, no. 12, American Chemical Society, 2009, pp. 4233–35, doi:10.1021/ja9001585.
short: R. Klajn, L. Fang, A. Coskun, M.A. Olson, P.J. Wesson, J.F. Stoddart, B.A.
Grzybowski, Journal of the American Chemical Society 131 (2009) 4233–4235.
date_created: 2023-08-01T10:30:17Z
date_published: 2009-04-01T00:00:00Z
date_updated: 2023-08-08T09:06:00Z
day: '01'
doi: 10.1021/ja9001585
extern: '1'
external_id:
pmid:
- '19265400'
intvolume: ' 131'
issue: '12'
keyword:
- Colloid and Surface Chemistry
- Biochemistry
- General Chemistry
- Catalysis
language:
- iso: eng
month: '04'
oa_version: None
page: 4233-4235
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: Metal nanoparticles functionalized with molecular and supramolecular switches
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: '13428'
abstract:
- lang: eng
text: Mixtures of oppositely charged nanoparticles of various sizes and charge ratios
precipitate only at the point of electroneutrality. This phenomenonspecific to
the nanoscale and reminiscent of threshold precipitation of ionsis a consequence
of the formation of core-and-shell nanoparticle aggregates, in which the shells
are composed of like-charged particles and are stabilized by efficient electrostatic
screening.
article_processing_charge: No
article_type: original
author:
- first_name: Alexander M.
full_name: Kalsin, Alexander M.
last_name: Kalsin
- first_name: Bartlomiej
full_name: Kowalczyk, Bartlomiej
last_name: Kowalczyk
- first_name: Stoyan K.
full_name: Smoukov, Stoyan K.
last_name: Smoukov
- first_name: Rafal
full_name: Klajn, Rafal
id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b
last_name: Klajn
- first_name: Bartosz A.
full_name: Grzybowski, Bartosz A.
last_name: Grzybowski
citation:
ama: Kalsin AM, Kowalczyk B, Smoukov SK, Klajn R, Grzybowski BA. Ionic-like behavior
of oppositely charged nanoparticles. Journal of the American Chemical Society.
2006;128(47):15046-15047. doi:10.1021/ja0642966
apa: Kalsin, A. M., Kowalczyk, B., Smoukov, S. K., Klajn, R., & Grzybowski,
B. A. (2006). Ionic-like behavior of oppositely charged nanoparticles. Journal
of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/ja0642966
chicago: Kalsin, Alexander M., Bartlomiej Kowalczyk, Stoyan K. Smoukov, Rafal Klajn,
and Bartosz A. Grzybowski. “Ionic-like Behavior of Oppositely Charged Nanoparticles.”
Journal of the American Chemical Society. American Chemical Society, 2006.
https://doi.org/10.1021/ja0642966.
ieee: A. M. Kalsin, B. Kowalczyk, S. K. Smoukov, R. Klajn, and B. A. Grzybowski,
“Ionic-like behavior of oppositely charged nanoparticles,” Journal of the American
Chemical Society, vol. 128, no. 47. American Chemical Society, pp. 15046–15047,
2006.
ista: Kalsin AM, Kowalczyk B, Smoukov SK, Klajn R, Grzybowski BA. 2006. Ionic-like
behavior of oppositely charged nanoparticles. Journal of the American Chemical
Society. 128(47), 15046–15047.
mla: Kalsin, Alexander M., et al. “Ionic-like Behavior of Oppositely Charged Nanoparticles.”
Journal of the American Chemical Society, vol. 128, no. 47, American Chemical
Society, 2006, pp. 15046–47, doi:10.1021/ja0642966.
short: A.M. Kalsin, B. Kowalczyk, S.K. Smoukov, R. Klajn, B.A. Grzybowski, Journal
of the American Chemical Society 128 (2006) 15046–15047.
date_created: 2023-08-01T10:36:27Z
date_published: 2006-11-29T00:00:00Z
date_updated: 2023-08-08T11:30:06Z
day: '29'
doi: 10.1021/ja0642966
extern: '1'
external_id:
pmid:
- '17117829'
intvolume: ' 128'
issue: '47'
keyword:
- Colloid and Surface Chemistry
- Biochemistry
- General Chemistry
- Catalysis
language:
- iso: eng
month: '11'
oa_version: None
page: 15046-15047
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: Ionic-like behavior of oppositely charged nanoparticles
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'
...