---
_id: '8441'
abstract:
- lang: eng
text: Solid-state near-rotary-resonance measurements of the spin–lattice relaxation
rate in the rotating frame (R1ρ) is a powerful NMR technique for studying molecular
dynamics in the microsecond time scale. The small difference between the spin-lock
(SL) and magic-angle-spinning (MAS) frequencies allows sampling very slow motions,
at the same time it brings up some methodological challenges. In this work, several
issues affecting correct measurements and analysis of 15N R1ρ data are considered
in detail. Among them are signal amplitude as a function of the difference between
SL and MAS frequencies, “dead time” in the initial part of the relaxation decay
caused by transient spin-dynamic oscillations, measurements under HORROR condition
and proper treatment of the multi-exponential relaxation decays. The multiple
15N R1ρ measurements at different SL fields and temperatures have been conducted
in 1D mode (i.e. without site-specific resolution) for a set of four different
microcrystalline protein samples (GB1, SH3, MPD-ubiquitin and cubic-PEG-ubiquitin)
to study the overall protein rocking in a crystal. While the amplitude of this
motion varies very significantly, its correlation time for all four sample is
practically the same, 30–50 μs. The amplitude of the rocking motion correlates
with the packing density of a protein crystal. It has been suggested that the
rocking motion is not diffusive but likely a jump-like dynamic process.
article_processing_charge: No
article_type: original
author:
- first_name: Alexey
full_name: Krushelnitsky, Alexey
last_name: Krushelnitsky
- first_name: Diego
full_name: Gauto, Diego
last_name: Gauto
- first_name: Diana C.
full_name: Rodriguez Camargo, Diana C.
last_name: Rodriguez Camargo
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Kay
full_name: Saalwächter, Kay
last_name: Saalwächter
citation:
ama: 'Krushelnitsky A, Gauto D, Rodriguez Camargo DC, Schanda P, Saalwächter K.
Microsecond motions probed by near-rotary-resonance R1ρ 15N MAS NMR experiments:
The model case of protein overall-rocking in crystals. Journal of Biomolecular
NMR. 2018;71(1):53-67. doi:10.1007/s10858-018-0191-4'
apa: 'Krushelnitsky, A., Gauto, D., Rodriguez Camargo, D. C., Schanda, P., &
Saalwächter, K. (2018). Microsecond motions probed by near-rotary-resonance R1ρ
15N MAS NMR experiments: The model case of protein overall-rocking in crystals.
Journal of Biomolecular NMR. Springer Nature. https://doi.org/10.1007/s10858-018-0191-4'
chicago: 'Krushelnitsky, Alexey, Diego Gauto, Diana C. Rodriguez Camargo, Paul Schanda,
and Kay Saalwächter. “Microsecond Motions Probed by Near-Rotary-Resonance R1ρ
15N MAS NMR Experiments: The Model Case of Protein Overall-Rocking in Crystals.”
Journal of Biomolecular NMR. Springer Nature, 2018. https://doi.org/10.1007/s10858-018-0191-4.'
ieee: 'A. Krushelnitsky, D. Gauto, D. C. Rodriguez Camargo, P. Schanda, and K. Saalwächter,
“Microsecond motions probed by near-rotary-resonance R1ρ 15N MAS NMR experiments:
The model case of protein overall-rocking in crystals,” Journal of Biomolecular
NMR, vol. 71, no. 1. Springer Nature, pp. 53–67, 2018.'
ista: 'Krushelnitsky A, Gauto D, Rodriguez Camargo DC, Schanda P, Saalwächter K.
2018. Microsecond motions probed by near-rotary-resonance R1ρ 15N MAS NMR experiments:
The model case of protein overall-rocking in crystals. Journal of Biomolecular
NMR. 71(1), 53–67.'
mla: 'Krushelnitsky, Alexey, et al. “Microsecond Motions Probed by Near-Rotary-Resonance
R1ρ 15N MAS NMR Experiments: The Model Case of Protein Overall-Rocking in Crystals.”
Journal of Biomolecular NMR, vol. 71, no. 1, Springer Nature, 2018, pp.
53–67, doi:10.1007/s10858-018-0191-4.'
short: A. Krushelnitsky, D. Gauto, D.C. Rodriguez Camargo, P. Schanda, K. Saalwächter,
Journal of Biomolecular NMR 71 (2018) 53–67.
date_created: 2020-09-18T10:05:28Z
date_published: 2018-05-30T00:00:00Z
date_updated: 2021-01-12T08:19:17Z
day: '30'
doi: 10.1007/s10858-018-0191-4
extern: '1'
intvolume: ' 71'
issue: '1'
language:
- iso: eng
month: '05'
oa_version: Published Version
page: 53-67
publication: Journal of Biomolecular NMR
publication_identifier:
issn:
- 0925-2738
- 1573-5001
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: 'Microsecond motions probed by near-rotary-resonance R1ρ 15N MAS NMR experiments:
The model case of protein overall-rocking in crystals'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 71
year: '2018'
...
---
_id: '8461'
abstract:
- lang: eng
text: Solid-state NMR provides insight into protein motion over time scales ranging
from picoseconds to seconds. While in solution state the methodology to measure
protein dynamics is well established, there is currently no such consensus protocol
for measuring dynamics in solids. In this article, we perform a detailed investigation
of measurement protocols for fast motions, i.e. motions ranging from picoseconds
to a few microseconds, which is the range covered by dipolar coupling and relaxation
experiments. We perform a detailed theoretical investigation how dipolar couplings
and relaxation data can provide information about amplitudes and time scales of
local motion. We show that the measurement of dipolar couplings is crucial for
obtaining accurate motional parameters, while systematic errors are found when
only relaxation data are used. Based on this realization, we investigate how the
REDOR experiment can provide such data in a very accurate manner. We identify
that with accurate rf calibration, and explicit consideration of rf field inhomogeneities,
one can obtain highly accurate absolute order parameters. We then perform joint
model-free analyses of 6 relaxation data sets and dipolar couplings, based on
previously existing, as well as new data sets on microcrystalline ubiquitin. We
show that nanosecond motion can be detected primarily in loop regions, and compare
solid-state data to solution-state relaxation and RDC analyses. The protocols
investigated here will serve as a useful basis towards the establishment of a
routine protocol for the characterization of ps–μs motions in proteins by solid-state
NMR.
article_processing_charge: No
article_type: original
author:
- first_name: Jens D.
full_name: Haller, Jens D.
last_name: Haller
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: 'Haller JD, Schanda P. Amplitudes and time scales of picosecond-to-microsecond
motion in proteins studied by solid-state NMR: a critical evaluation of experimental
approaches and application to crystalline ubiquitin. Journal of Biomolecular
NMR. 2013;57(3):263-280. doi:10.1007/s10858-013-9787-x'
apa: 'Haller, J. D., & Schanda, P. (2013). Amplitudes and time scales of picosecond-to-microsecond
motion in proteins studied by solid-state NMR: a critical evaluation of experimental
approaches and application to crystalline ubiquitin. Journal of Biomolecular
NMR. Springer Nature. https://doi.org/10.1007/s10858-013-9787-x'
chicago: 'Haller, Jens D., and Paul Schanda. “Amplitudes and Time Scales of Picosecond-to-Microsecond
Motion in Proteins Studied by Solid-State NMR: A Critical Evaluation of Experimental
Approaches and Application to Crystalline Ubiquitin.” Journal of Biomolecular
NMR. Springer Nature, 2013. https://doi.org/10.1007/s10858-013-9787-x.'
ieee: 'J. D. Haller and P. Schanda, “Amplitudes and time scales of picosecond-to-microsecond
motion in proteins studied by solid-state NMR: a critical evaluation of experimental
approaches and application to crystalline ubiquitin,” Journal of Biomolecular
NMR, vol. 57, no. 3. Springer Nature, pp. 263–280, 2013.'
ista: 'Haller JD, Schanda P. 2013. Amplitudes and time scales of picosecond-to-microsecond
motion in proteins studied by solid-state NMR: a critical evaluation of experimental
approaches and application to crystalline ubiquitin. Journal of Biomolecular NMR.
57(3), 263–280.'
mla: 'Haller, Jens D., and Paul Schanda. “Amplitudes and Time Scales of Picosecond-to-Microsecond
Motion in Proteins Studied by Solid-State NMR: A Critical Evaluation of Experimental
Approaches and Application to Crystalline Ubiquitin.” Journal of Biomolecular
NMR, vol. 57, no. 3, Springer Nature, 2013, pp. 263–80, doi:10.1007/s10858-013-9787-x.'
short: J.D. Haller, P. Schanda, Journal of Biomolecular NMR 57 (2013) 263–280.
date_created: 2020-09-18T10:09:05Z
date_published: 2013-10-09T00:00:00Z
date_updated: 2021-01-12T08:19:26Z
day: '09'
doi: 10.1007/s10858-013-9787-x
extern: '1'
intvolume: ' 57'
issue: '3'
keyword:
- Spectroscopy
- Biochemistry
language:
- iso: eng
month: '10'
oa_version: None
page: 263-280
publication: Journal of Biomolecular NMR
publication_identifier:
issn:
- 0925-2738
- 1573-5001
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: 'Amplitudes and time scales of picosecond-to-microsecond motion in proteins
studied by solid-state NMR: a critical evaluation of experimental approaches and
application to crystalline ubiquitin'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 57
year: '2013'
...
---
_id: '8463'
abstract:
- lang: eng
text: The 1H dipolar network, which is the major obstacle for applying proton detection
in the solid-state, can be reduced by deuteration, employing the RAP (Reduced
Adjoining Protonation) labeling scheme, which yields random protonation at non-exchangeable
sites. We present here a systematic study on the optimal degree of random sidechain
protonation in RAP samples as a function of the MAS (magic angle spinning) frequency.
In particular, we compare 1H sensitivity and linewidth of a microcrystalline protein,
the SH3 domain of chicken α-spectrin, for samples, prepared with 5–25 % H2O in
the E. coli growth medium, in the MAS frequency range of 20–60 kHz. At an external
field of 19.96 T (850 MHz), we find that using a proton concentration between
15 and 25 % in the M9 medium yields the best compromise in terms of sensitivity
and resolution, with an achievable average 1H linewidth on the order of 40–50
Hz. Comparing sensitivities at a MAS frequency of 60 versus 20 kHz, a gain in
sensitivity by a factor of 4–4.5 is observed in INEPT-based 1H detected 1D 1H,13C
correlation experiments. In total, we find that spectra recorded with a 1.3 mm
rotor at 60 kHz have almost the same sensitivity as spectra recorded with a fully
packed 3.2 mm rotor at 20 kHz, even though ~20× less material is employed. The
improved sensitivity is attributed to 1H line narrowing due to fast MAS and to
the increased efficiency of the 1.3 mm coil.
article_processing_charge: No
article_type: original
author:
- first_name: Sam
full_name: Asami, Sam
last_name: Asami
- first_name: Kathrin
full_name: Szekely, Kathrin
last_name: Szekely
- 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: Bernd
full_name: Reif, Bernd
last_name: Reif
citation:
ama: Asami S, Szekely K, Schanda P, Meier BH, Reif B. Optimal degree of protonation
for 1H detection of aliphatic sites in randomly deuterated proteins as a function
of the MAS frequency. Journal of Biomolecular NMR. 2012;54(2):155-168.
doi:10.1007/s10858-012-9659-9
apa: Asami, S., Szekely, K., Schanda, P., Meier, B. H., & Reif, B. (2012). Optimal
degree of protonation for 1H detection of aliphatic sites in randomly deuterated
proteins as a function of the MAS frequency. Journal of Biomolecular NMR.
Springer Nature. https://doi.org/10.1007/s10858-012-9659-9
chicago: Asami, Sam, Kathrin Szekely, Paul Schanda, Beat H. Meier, and Bernd Reif.
“Optimal Degree of Protonation for 1H Detection of Aliphatic Sites in Randomly
Deuterated Proteins as a Function of the MAS Frequency.” Journal of Biomolecular
NMR. Springer Nature, 2012. https://doi.org/10.1007/s10858-012-9659-9.
ieee: S. Asami, K. Szekely, P. Schanda, B. H. Meier, and B. Reif, “Optimal degree
of protonation for 1H detection of aliphatic sites in randomly deuterated proteins
as a function of the MAS frequency,” Journal of Biomolecular NMR, vol.
54, no. 2. Springer Nature, pp. 155–168, 2012.
ista: Asami S, Szekely K, Schanda P, Meier BH, Reif B. 2012. Optimal degree of protonation
for 1H detection of aliphatic sites in randomly deuterated proteins as a function
of the MAS frequency. Journal of Biomolecular NMR. 54(2), 155–168.
mla: Asami, Sam, et al. “Optimal Degree of Protonation for 1H Detection of Aliphatic
Sites in Randomly Deuterated Proteins as a Function of the MAS Frequency.” Journal
of Biomolecular NMR, vol. 54, no. 2, Springer Nature, 2012, pp. 155–68, doi:10.1007/s10858-012-9659-9.
short: S. Asami, K. Szekely, P. Schanda, B.H. Meier, B. Reif, Journal of Biomolecular
NMR 54 (2012) 155–168.
date_created: 2020-09-18T10:09:18Z
date_published: 2012-08-23T00:00:00Z
date_updated: 2021-01-12T08:19:27Z
day: '23'
doi: 10.1007/s10858-012-9659-9
extern: '1'
intvolume: ' 54'
issue: '2'
language:
- iso: eng
month: '08'
oa_version: None
page: 155-168
publication: Journal of Biomolecular NMR
publication_identifier:
issn:
- 0925-2738
- 1573-5001
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: Optimal degree of protonation for 1H detection of aliphatic sites in randomly
deuterated proteins as a function of the MAS frequency
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 54
year: '2012'
...
---
_id: '8468'
article_processing_charge: No
article_type: original
author:
- first_name: Daniela
full_name: Lalli, Daniela
last_name: Lalli
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Anup
full_name: Chowdhury, Anup
last_name: Chowdhury
- first_name: Joren
full_name: Retel, Joren
last_name: Retel
- first_name: Matthias
full_name: Hiller, Matthias
last_name: Hiller
- first_name: Victoria A.
full_name: Higman, Victoria A.
last_name: Higman
- first_name: Lieselotte
full_name: Handel, Lieselotte
last_name: Handel
- first_name: Vipin
full_name: Agarwal, Vipin
last_name: Agarwal
- first_name: Bernd
full_name: Reif, Bernd
last_name: Reif
- first_name: Barth
full_name: van Rossum, Barth
last_name: van Rossum
- first_name: Ümit
full_name: Akbey, Ümit
last_name: Akbey
- first_name: Hartmut
full_name: Oschkinat, Hartmut
last_name: Oschkinat
citation:
ama: Lalli D, Schanda P, Chowdhury A, et al. Three-dimensional deuterium-carbon
correlation experiments for high-resolution solid-state MAS NMR spectroscopy of
large proteins. Journal of Biomolecular NMR. 2011;51(4):477-485. doi:10.1007/s10858-011-9578-1
apa: Lalli, D., Schanda, P., Chowdhury, A., Retel, J., Hiller, M., Higman, V. A.,
… Oschkinat, H. (2011). Three-dimensional deuterium-carbon correlation experiments
for high-resolution solid-state MAS NMR spectroscopy of large proteins. Journal
of Biomolecular NMR. Springer Nature. https://doi.org/10.1007/s10858-011-9578-1
chicago: Lalli, Daniela, Paul Schanda, Anup Chowdhury, Joren Retel, Matthias Hiller,
Victoria A. Higman, Lieselotte Handel, et al. “Three-Dimensional Deuterium-Carbon
Correlation Experiments for High-Resolution Solid-State MAS NMR Spectroscopy of
Large Proteins.” Journal of Biomolecular NMR. Springer Nature, 2011. https://doi.org/10.1007/s10858-011-9578-1.
ieee: D. Lalli et al., “Three-dimensional deuterium-carbon correlation experiments
for high-resolution solid-state MAS NMR spectroscopy of large proteins,” Journal
of Biomolecular NMR, vol. 51, no. 4. Springer Nature, pp. 477–485, 2011.
ista: Lalli D, Schanda P, Chowdhury A, Retel J, Hiller M, Higman VA, Handel L, Agarwal
V, Reif B, van Rossum B, Akbey Ü, Oschkinat H. 2011. Three-dimensional deuterium-carbon
correlation experiments for high-resolution solid-state MAS NMR spectroscopy of
large proteins. Journal of Biomolecular NMR. 51(4), 477–485.
mla: Lalli, Daniela, et al. “Three-Dimensional Deuterium-Carbon Correlation Experiments
for High-Resolution Solid-State MAS NMR Spectroscopy of Large Proteins.” Journal
of Biomolecular NMR, vol. 51, no. 4, Springer Nature, 2011, pp. 477–85, doi:10.1007/s10858-011-9578-1.
short: D. Lalli, P. Schanda, A. Chowdhury, J. Retel, M. Hiller, V.A. Higman, L.
Handel, V. Agarwal, B. Reif, B. van Rossum, Ü. Akbey, H. Oschkinat, Journal of
Biomolecular NMR 51 (2011) 477–485.
date_created: 2020-09-18T10:10:43Z
date_published: 2011-10-25T00:00:00Z
date_updated: 2021-01-12T08:19:29Z
day: '25'
doi: 10.1007/s10858-011-9578-1
extern: '1'
intvolume: ' 51'
issue: '4'
language:
- iso: eng
month: '10'
oa_version: None
page: 477-485
publication: Journal of Biomolecular NMR
publication_identifier:
issn:
- 0925-2738
- 1573-5001
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: Three-dimensional deuterium-carbon correlation experiments for high-resolution
solid-state MAS NMR spectroscopy of large proteins
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 51
year: '2011'
...
---
_id: '8479'
abstract:
- lang: eng
text: Multidimensional NMR spectroscopy is a well-established technique for the
characterization of structure and fast-time-scale dynamics of highly populated
ground states of biological macromolecules. The investigation of short-lived excited
states that are important for molecular folding, misfolding and function, however,
remains a challenge for modern biomolecular NMR techniques. Off-equilibrium real-time
kinetic NMR methods allow direct observation of conformational or chemical changes
by following peak positions and intensities in a series of spectra recorded during
a kinetic event. Because standard multidimensional NMR methods required to yield
sufficient atom-resolution are intrinsically time-consuming, many interesting
phenomena are excluded from real-time NMR analysis. Recently, spatially encoded
ultrafast 2D NMR techniques have been proposed that allow one to acquire a 2D
NMR experiment within a single transient. In addition, when combined with the
SOFAST technique, such ultrafast experiments can be repeated at high rates. One
of the problems detected for such ultrafast protein NMR experiments is related
to the heteronuclear decoupling during detection with interferences between the
pulses and the oscillatory magnetic field gradients arising in this scheme. Here
we present a method for improved ultrafast data acquisition yielding higher signal
to noise and sharper lines in single-scan 2D NMR spectra. In combination with
a fast-mixing device, the recording of 1H–15N correlation spectra with repetition
rates of up to a few Hertz becomes feasible, enabling real-time studies of protein
kinetics occurring on time scales down to a few seconds.
article_processing_charge: No
article_type: original
author:
- first_name: Maayan
full_name: Gal, Maayan
last_name: Gal
- first_name: Thomas
full_name: Kern, Thomas
last_name: Kern
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Lucio
full_name: Frydman, Lucio
last_name: Frydman
- first_name: Bernhard
full_name: Brutscher, Bernhard
last_name: Brutscher
citation:
ama: 'Gal M, Kern T, Schanda P, Frydman L, Brutscher B. An improved ultrafast 2D
NMR experiment: Towards atom-resolved real-time studies of protein kinetics at
multi-Hz rates. Journal of Biomolecular NMR. 2009;43:1-10. doi:10.1007/s10858-008-9284-9'
apa: 'Gal, M., Kern, T., Schanda, P., Frydman, L., & Brutscher, B. (2009). An
improved ultrafast 2D NMR experiment: Towards atom-resolved real-time studies
of protein kinetics at multi-Hz rates. Journal of Biomolecular NMR. Springer
Nature. https://doi.org/10.1007/s10858-008-9284-9'
chicago: 'Gal, Maayan, Thomas Kern, Paul Schanda, Lucio Frydman, and Bernhard Brutscher.
“An Improved Ultrafast 2D NMR Experiment: Towards Atom-Resolved Real-Time Studies
of Protein Kinetics at Multi-Hz Rates.” Journal of Biomolecular NMR. Springer
Nature, 2009. https://doi.org/10.1007/s10858-008-9284-9.'
ieee: 'M. Gal, T. Kern, P. Schanda, L. Frydman, and B. Brutscher, “An improved ultrafast
2D NMR experiment: Towards atom-resolved real-time studies of protein kinetics
at multi-Hz rates,” Journal of Biomolecular NMR, vol. 43. Springer Nature,
pp. 1–10, 2009.'
ista: 'Gal M, Kern T, Schanda P, Frydman L, Brutscher B. 2009. An improved ultrafast
2D NMR experiment: Towards atom-resolved real-time studies of protein kinetics
at multi-Hz rates. Journal of Biomolecular NMR. 43, 1–10.'
mla: 'Gal, Maayan, et al. “An Improved Ultrafast 2D NMR Experiment: Towards Atom-Resolved
Real-Time Studies of Protein Kinetics at Multi-Hz Rates.” Journal of Biomolecular
NMR, vol. 43, Springer Nature, 2009, pp. 1–10, doi:10.1007/s10858-008-9284-9.'
short: M. Gal, T. Kern, P. Schanda, L. Frydman, B. Brutscher, Journal of Biomolecular
NMR 43 (2009) 1–10.
date_created: 2020-09-18T10:12:20Z
date_published: 2009-01-01T00:00:00Z
date_updated: 2021-01-12T08:19:33Z
day: '01'
doi: 10.1007/s10858-008-9284-9
extern: '1'
intvolume: ' 43'
keyword:
- Spectroscopy
- Biochemistry
language:
- iso: eng
month: '01'
oa_version: None
page: 1-10
publication: Journal of Biomolecular NMR
publication_identifier:
issn:
- 0925-2738
- 1573-5001
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: 'An improved ultrafast 2D NMR experiment: Towards atom-resolved real-time studies
of protein kinetics at multi-Hz rates'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 43
year: '2009'
...
---
_id: '8485'
abstract:
- lang: eng
text: High signal to noise is a necessity for the quantification of NMR spectral
parameters to be translated into accurate and precise restraints on protein structure
and dynamics. An important source of long-range structural information is obtained
from 1H–1H residual dipolar couplings (RDCs) measured for weakly aligned molecules.
For sensitivity reasons, such measurements are generally performed on highly deuterated
protein samples. Here we show that high sensitivity is also obtained for protonated
protein samples if the pulse schemes are optimized in terms of longitudinal relaxation
efficiency and J-mismatch compensated coherence transfer. The new sensitivity-optimized
quantitative J-correlation experiment yields important signal gains reaching factors
of 1.5 to 8 for individual correlation peaks when compared to previously proposed
pulse schemes.
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: Ewen
full_name: Lescop, Ewen
last_name: Lescop
- first_name: Mirjam
full_name: Falge, Mirjam
last_name: Falge
- first_name: Rémy
full_name: Sounier, Rémy
last_name: Sounier
- first_name: Jérôme
full_name: Boisbouvier, Jérôme
last_name: Boisbouvier
- first_name: Bernhard
full_name: Brutscher, Bernhard
last_name: Brutscher
citation:
ama: Schanda P, Lescop E, Falge M, Sounier R, Boisbouvier J, Brutscher B. Sensitivity-optimized
experiment for the measurement of residual dipolar couplings between amide protons.
Journal of Biomolecular NMR. 2007;38:47-55. doi:10.1007/s10858-006-9138-2
apa: Schanda, P., Lescop, E., Falge, M., Sounier, R., Boisbouvier, J., & Brutscher,
B. (2007). Sensitivity-optimized experiment for the measurement of residual dipolar
couplings between amide protons. Journal of Biomolecular NMR. Springer
Nature. https://doi.org/10.1007/s10858-006-9138-2
chicago: Schanda, Paul, Ewen Lescop, Mirjam Falge, Rémy Sounier, Jérôme Boisbouvier,
and Bernhard Brutscher. “Sensitivity-Optimized Experiment for the Measurement
of Residual Dipolar Couplings between Amide Protons.” Journal of Biomolecular
NMR. Springer Nature, 2007. https://doi.org/10.1007/s10858-006-9138-2.
ieee: P. Schanda, E. Lescop, M. Falge, R. Sounier, J. Boisbouvier, and B. Brutscher,
“Sensitivity-optimized experiment for the measurement of residual dipolar couplings
between amide protons,” Journal of Biomolecular NMR, vol. 38. Springer
Nature, pp. 47–55, 2007.
ista: Schanda P, Lescop E, Falge M, Sounier R, Boisbouvier J, Brutscher B. 2007.
Sensitivity-optimized experiment for the measurement of residual dipolar couplings
between amide protons. Journal of Biomolecular NMR. 38, 47–55.
mla: Schanda, Paul, et al. “Sensitivity-Optimized Experiment for the Measurement
of Residual Dipolar Couplings between Amide Protons.” Journal of Biomolecular
NMR, vol. 38, Springer Nature, 2007, pp. 47–55, doi:10.1007/s10858-006-9138-2.
short: P. Schanda, E. Lescop, M. Falge, R. Sounier, J. Boisbouvier, B. Brutscher,
Journal of Biomolecular NMR 38 (2007) 47–55.
date_created: 2020-09-18T10:13:12Z
date_published: 2007-03-08T00:00:00Z
date_updated: 2021-01-12T08:19:36Z
day: '08'
doi: 10.1007/s10858-006-9138-2
extern: '1'
intvolume: ' 38'
keyword:
- Spectroscopy
- Biochemistry
language:
- iso: eng
month: '03'
oa_version: None
page: 47-55
publication: Journal of Biomolecular NMR
publication_identifier:
issn:
- 0925-2738
- 1573-5001
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: Sensitivity-optimized experiment for the measurement of residual dipolar couplings
between amide protons
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 38
year: '2007'
...
---
_id: '8491'
abstract:
- lang: eng
text: Fast multidimensional NMR with a time resolution of a few seconds provides
a new tool for high throughput screening and site-resolved real-time studies of
kinetic molecular processes by NMR. Recently we have demonstrated the feasibility
to record protein 1H–15N correlation spectra in a few seconds of acquisition time
using a new SOFAST-HMQC experiment (Schanda and Brutscher (2005) J. Am. Chem.
Soc. 127, 8014). Here, we investigate in detail the performance of SOFAST-HMQC
to record 1H–15N and 1H−13C correlation spectra of proteins of different size
and at different magnetic field strengths. Compared to standard 1H–15N correlation
experiments SOFAST-HMQC provides a significant gain in sensitivity, especially
for fast repetition rates. Guidelines are provided on how to set up SOFAST-HMQC
experiments for a given protein sample. In addition, an alternative pulse scheme,
IPAP-SOFAST-HMQC is presented that allows application on NMR spectrometers equipped
with cryogenic probes, and fast measurement of one-bond 1H–13C and 1H–15N scalar
and residual dipolar coupling constants.
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: Ēriks
full_name: Kupče, Ēriks
last_name: Kupče
- first_name: Bernhard
full_name: Brutscher, Bernhard
last_name: Brutscher
citation:
ama: Schanda P, Kupče Ē, Brutscher B. SOFAST-HMQC experiments for recording two-dimensional
deteronuclear correlation spectra of proteins within a few seconds. Journal
of Biomolecular NMR. 2005;33(4):199-211. doi:10.1007/s10858-005-4425-x
apa: Schanda, P., Kupče, Ē., & Brutscher, B. (2005). SOFAST-HMQC experiments
for recording two-dimensional deteronuclear correlation spectra of proteins within
a few seconds. Journal of Biomolecular NMR. Springer Nature. https://doi.org/10.1007/s10858-005-4425-x
chicago: Schanda, Paul, Ēriks Kupče, and Bernhard Brutscher. “SOFAST-HMQC Experiments
for Recording Two-Dimensional Deteronuclear Correlation Spectra of Proteins within
a Few Seconds.” Journal of Biomolecular NMR. Springer Nature, 2005. https://doi.org/10.1007/s10858-005-4425-x.
ieee: P. Schanda, Ē. Kupče, and B. Brutscher, “SOFAST-HMQC experiments for recording
two-dimensional deteronuclear correlation spectra of proteins within a few seconds,”
Journal of Biomolecular NMR, vol. 33, no. 4. Springer Nature, pp. 199–211,
2005.
ista: Schanda P, Kupče Ē, Brutscher B. 2005. SOFAST-HMQC experiments for recording
two-dimensional deteronuclear correlation spectra of proteins within a few seconds.
Journal of Biomolecular NMR. 33(4), 199–211.
mla: Schanda, Paul, et al. “SOFAST-HMQC Experiments for Recording Two-Dimensional
Deteronuclear Correlation Spectra of Proteins within a Few Seconds.” Journal
of Biomolecular NMR, vol. 33, no. 4, Springer Nature, 2005, pp. 199–211, doi:10.1007/s10858-005-4425-x.
short: P. Schanda, Ē. Kupče, B. Brutscher, Journal of Biomolecular NMR 33 (2005)
199–211.
date_created: 2020-09-18T10:13:59Z
date_published: 2005-12-01T00:00:00Z
date_updated: 2021-01-12T08:19:38Z
day: '01'
doi: 10.1007/s10858-005-4425-x
extern: '1'
intvolume: ' 33'
issue: '4'
keyword:
- Spectroscopy
- Biochemistry
language:
- iso: eng
month: '12'
oa_version: None
page: 199-211
publication: Journal of Biomolecular NMR
publication_identifier:
issn:
- 0925-2738
- 1573-5001
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: SOFAST-HMQC experiments for recording two-dimensional deteronuclear correlation
spectra of proteins within a few seconds
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 33
year: '2005'
...