---
_id: '8407'
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
citation:
  ama: Schanda P. Relaxing with liquids and solids – A perspective on biomolecular
    dynamics. <i>Journal of Magnetic Resonance</i>. 2019;306:180-186. doi:<a href="https://doi.org/10.1016/j.jmr.2019.07.025">10.1016/j.jmr.2019.07.025</a>
  apa: Schanda, P. (2019). Relaxing with liquids and solids – A perspective on biomolecular
    dynamics. <i>Journal of Magnetic Resonance</i>. Elsevier. <a href="https://doi.org/10.1016/j.jmr.2019.07.025">https://doi.org/10.1016/j.jmr.2019.07.025</a>
  chicago: Schanda, Paul. “Relaxing with Liquids and Solids – A Perspective on Biomolecular
    Dynamics.” <i>Journal of Magnetic Resonance</i>. Elsevier, 2019. <a href="https://doi.org/10.1016/j.jmr.2019.07.025">https://doi.org/10.1016/j.jmr.2019.07.025</a>.
  ieee: P. Schanda, “Relaxing with liquids and solids – A perspective on biomolecular
    dynamics,” <i>Journal of Magnetic Resonance</i>, vol. 306. Elsevier, pp. 180–186,
    2019.
  ista: Schanda P. 2019. Relaxing with liquids and solids – A perspective on biomolecular
    dynamics. Journal of Magnetic Resonance. 306, 180–186.
  mla: Schanda, Paul. “Relaxing with Liquids and Solids – A Perspective on Biomolecular
    Dynamics.” <i>Journal of Magnetic Resonance</i>, vol. 306, Elsevier, 2019, pp.
    180–86, doi:<a href="https://doi.org/10.1016/j.jmr.2019.07.025">10.1016/j.jmr.2019.07.025</a>.
  short: P. Schanda, Journal of Magnetic Resonance 306 (2019) 180–186.
date_created: 2020-09-17T10:28:47Z
date_published: 2019-09-01T00:00:00Z
date_updated: 2021-01-12T08:19:04Z
day: '01'
doi: 10.1016/j.jmr.2019.07.025
extern: '1'
external_id:
  pmid:
  - '31350165'
intvolume: '       306'
keyword:
- Nuclear and High Energy Physics
- Biophysics
- Biochemistry
- Condensed Matter Physics
language:
- iso: eng
month: '09'
oa_version: Submitted Version
page: 180-186
pmid: 1
publication: Journal of Magnetic Resonance
publication_identifier:
  issn:
  - 1090-7807
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: Relaxing with liquids and solids – A perspective on biomolecular dynamics
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 306
year: '2019'
...
---
_id: '8448'
abstract:
- lang: eng
  text: We present an improved fast mixing device based on the rapid mixing of two
    solutions inside the NMR probe, as originally proposed by Hore and coworkers (J.
    Am. Chem. Soc. 125 (2003) 12484–12492). Such a device is important for off-equilibrium
    studies of molecular kinetics by multidimensional real-time NMR spectrsocopy.
    The novelty of this device is that it allows removing the injector from the NMR
    detection volume after mixing, and thus provides good magnetic field homogeneity
    independently of the initial sample volume placed in the NMR probe. The apparatus
    is simple to build, inexpensive, and can be used without any hardware modification
    on any type of liquid-state NMR spectrometer. We demonstrate the performance of
    our fast mixing device in terms of improved magnetic field homogeneity, and show
    an application to the study of protein folding and the structural characterization
    of transiently populated folding intermediates.
article_processing_charge: No
article_type: original
author:
- first_name: Rémi
  full_name: Franco, Rémi
  last_name: Franco
- first_name: Adrien
  full_name: Favier, Adrien
  last_name: Favier
- 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: Franco R, Favier A, Schanda P, Brutscher B. Optimized fast mixing device for
    real-time NMR applications. <i>Journal of Magnetic Resonance</i>. 2017;281(8):125-129.
    doi:<a href="https://doi.org/10.1016/j.jmr.2017.05.016">10.1016/j.jmr.2017.05.016</a>
  apa: Franco, R., Favier, A., Schanda, P., &#38; Brutscher, B. (2017). Optimized
    fast mixing device for real-time NMR applications. <i>Journal of Magnetic Resonance</i>.
    Elsevier. <a href="https://doi.org/10.1016/j.jmr.2017.05.016">https://doi.org/10.1016/j.jmr.2017.05.016</a>
  chicago: Franco, Rémi, Adrien Favier, Paul Schanda, and Bernhard Brutscher. “Optimized
    Fast Mixing Device for Real-Time NMR Applications.” <i>Journal of Magnetic Resonance</i>.
    Elsevier, 2017. <a href="https://doi.org/10.1016/j.jmr.2017.05.016">https://doi.org/10.1016/j.jmr.2017.05.016</a>.
  ieee: R. Franco, A. Favier, P. Schanda, and B. Brutscher, “Optimized fast mixing
    device for real-time NMR applications,” <i>Journal of Magnetic Resonance</i>,
    vol. 281, no. 8. Elsevier, pp. 125–129, 2017.
  ista: Franco R, Favier A, Schanda P, Brutscher B. 2017. Optimized fast mixing device
    for real-time NMR applications. Journal of Magnetic Resonance. 281(8), 125–129.
  mla: Franco, Rémi, et al. “Optimized Fast Mixing Device for Real-Time NMR Applications.”
    <i>Journal of Magnetic Resonance</i>, vol. 281, no. 8, Elsevier, 2017, pp. 125–29,
    doi:<a href="https://doi.org/10.1016/j.jmr.2017.05.016">10.1016/j.jmr.2017.05.016</a>.
  short: R. Franco, A. Favier, P. Schanda, B. Brutscher, Journal of Magnetic Resonance
    281 (2017) 125–129.
date_created: 2020-09-18T10:06:27Z
date_published: 2017-08-01T00:00:00Z
date_updated: 2021-01-12T08:19:20Z
day: '01'
doi: 10.1016/j.jmr.2017.05.016
extern: '1'
intvolume: '       281'
issue: '8'
keyword:
- Nuclear and High Energy Physics
- Biophysics
- Biochemistry
- Condensed Matter Physics
language:
- iso: eng
month: '08'
oa_version: None
page: 125-129
publication: Journal of Magnetic Resonance
publication_identifier:
  issn:
  - 1090-7807
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: Optimized fast mixing device for real-time NMR applications
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 281
year: '2017'
...
---
_id: '8467'
abstract:
- lang: eng
  text: Partial deuteration is a powerful tool to increase coherence life times and
    spectral resolution in proton solid-state NMR. The J coupling to deuterium needs,
    however, to be decoupled to maintain the good resolution in the (usually indirect)
    13C dimension(s). We present a simple and reversible way to expand a commercial
    1.3 mm HCN MAS probe with a 2H channel with sufficient field strength for J-decoupling
    of deuterium, namely 2–3 kHz. The coil is placed at the outside of the stator
    and requires no significant modifications to the probe. The performance and the
    realizable gains in sensitivity and resolution are demonstrated using perdeuterated
    ubiquitin, with selectively CHD2-labeled methyl groups.
article_processing_charge: No
article_type: original
author:
- first_name: Matthias
  full_name: Huber, Matthias
  last_name: Huber
- first_name: Oliver
  full_name: With, Oliver
  last_name: With
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
- first_name: René
  full_name: Verel, René
  last_name: Verel
- first_name: Matthias
  full_name: Ernst, Matthias
  last_name: Ernst
- first_name: Beat H.
  full_name: Meier, Beat H.
  last_name: Meier
citation:
  ama: Huber M, With O, Schanda P, Verel R, Ernst M, Meier BH. A supplementary coil
    for 2H decoupling with commercial HCN MAS probes. <i>Journal of Magnetic Resonance</i>.
    2012;214:76-80. doi:<a href="https://doi.org/10.1016/j.jmr.2011.10.010">10.1016/j.jmr.2011.10.010</a>
  apa: Huber, M., With, O., Schanda, P., Verel, R., Ernst, M., &#38; Meier, B. H.
    (2012). A supplementary coil for 2H decoupling with commercial HCN MAS probes.
    <i>Journal of Magnetic Resonance</i>. Elsevier. <a href="https://doi.org/10.1016/j.jmr.2011.10.010">https://doi.org/10.1016/j.jmr.2011.10.010</a>
  chicago: Huber, Matthias, Oliver With, Paul Schanda, René Verel, Matthias Ernst,
    and Beat H. Meier. “A Supplementary Coil for 2H Decoupling with Commercial HCN
    MAS Probes.” <i>Journal of Magnetic Resonance</i>. Elsevier, 2012. <a href="https://doi.org/10.1016/j.jmr.2011.10.010">https://doi.org/10.1016/j.jmr.2011.10.010</a>.
  ieee: M. Huber, O. With, P. Schanda, R. Verel, M. Ernst, and B. H. Meier, “A supplementary
    coil for 2H decoupling with commercial HCN MAS probes,” <i>Journal of Magnetic
    Resonance</i>, vol. 214. Elsevier, pp. 76–80, 2012.
  ista: Huber M, With O, Schanda P, Verel R, Ernst M, Meier BH. 2012. A supplementary
    coil for 2H decoupling with commercial HCN MAS probes. Journal of Magnetic Resonance.
    214, 76–80.
  mla: Huber, Matthias, et al. “A Supplementary Coil for 2H Decoupling with Commercial
    HCN MAS Probes.” <i>Journal of Magnetic Resonance</i>, vol. 214, Elsevier, 2012,
    pp. 76–80, doi:<a href="https://doi.org/10.1016/j.jmr.2011.10.010">10.1016/j.jmr.2011.10.010</a>.
  short: M. Huber, O. With, P. Schanda, R. Verel, M. Ernst, B.H. Meier, Journal of
    Magnetic Resonance 214 (2012) 76–80.
date_created: 2020-09-18T10:10:36Z
date_published: 2012-01-01T00:00:00Z
date_updated: 2021-01-12T08:19:28Z
day: '01'
doi: 10.1016/j.jmr.2011.10.010
extern: '1'
intvolume: '       214'
language:
- iso: eng
month: '01'
oa_version: None
page: 76-80
publication: Journal of Magnetic Resonance
publication_identifier:
  issn:
  - 1090-7807
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: A supplementary coil for 2H decoupling with commercial HCN MAS probes
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 214
year: '2012'
...
---
_id: '8469'
abstract:
- lang: eng
  text: The accurate experimental determination of dipolar-coupling constants for
    one-bond heteronuclear dipolar couplings in solids is a key for the quantification
    of the amplitudes of motional processes. Averaging of the dipolar coupling reports
    on motions on time scales up to the inverse of the coupling constant, in our case
    tens of microseconds. Combining dipolar-coupling derived order parameters that
    characterize the amplitudes of the motion with relaxation data leads to a more
    precise characterization of the dynamical parameters and helps to disentangle
    the amplitudes and the time scales of the motional processes, which impact relaxation
    rates in a highly correlated way. Here. we describe and characterize an improved
    experimental protocol – based on REDOR – to measure these couplings in perdeuterated
    proteins with a reduced sensitivity to experimental missettings. Because such
    effects are presently the dominant source of systematic errors in experimental
    dipolar-coupling measurements, these compensated experiments should help to significantly
    improve the precision of such data. A detailed comparison with other commonly
    used pulse sequences (T-MREV, phase-inverted CP,R18 5/2, and R18 7/1) is provided.
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. Accurate measurement of one-bond H–X heteronuclear
    dipolar couplings in MAS solid-state NMR. <i>Journal of Magnetic Resonance</i>.
    2011;210(2):246-259. doi:<a href="https://doi.org/10.1016/j.jmr.2011.03.015">10.1016/j.jmr.2011.03.015</a>
  apa: Schanda, P., Meier, B. H., &#38; Ernst, M. (2011). Accurate measurement of
    one-bond H–X heteronuclear dipolar couplings in MAS solid-state NMR. <i>Journal
    of Magnetic Resonance</i>. Elsevier. <a href="https://doi.org/10.1016/j.jmr.2011.03.015">https://doi.org/10.1016/j.jmr.2011.03.015</a>
  chicago: Schanda, Paul, Beat H. Meier, and Matthias Ernst. “Accurate Measurement
    of One-Bond H–X Heteronuclear Dipolar Couplings in MAS Solid-State NMR.” <i>Journal
    of Magnetic Resonance</i>. Elsevier, 2011. <a href="https://doi.org/10.1016/j.jmr.2011.03.015">https://doi.org/10.1016/j.jmr.2011.03.015</a>.
  ieee: P. Schanda, B. H. Meier, and M. Ernst, “Accurate measurement of one-bond H–X
    heteronuclear dipolar couplings in MAS solid-state NMR,” <i>Journal of Magnetic
    Resonance</i>, vol. 210, no. 2. Elsevier, pp. 246–259, 2011.
  ista: Schanda P, Meier BH, Ernst M. 2011. Accurate measurement of one-bond H–X heteronuclear
    dipolar couplings in MAS solid-state NMR. Journal of Magnetic Resonance. 210(2),
    246–259.
  mla: Schanda, Paul, et al. “Accurate Measurement of One-Bond H–X Heteronuclear Dipolar
    Couplings in MAS Solid-State NMR.” <i>Journal of Magnetic Resonance</i>, vol.
    210, no. 2, Elsevier, 2011, pp. 246–59, doi:<a href="https://doi.org/10.1016/j.jmr.2011.03.015">10.1016/j.jmr.2011.03.015</a>.
  short: P. Schanda, B.H. Meier, M. Ernst, Journal of Magnetic Resonance 210 (2011)
    246–259.
date_created: 2020-09-18T10:10:50Z
date_published: 2011-06-01T00:00:00Z
date_updated: 2021-01-12T08:19:29Z
day: '01'
doi: 10.1016/j.jmr.2011.03.015
extern: '1'
intvolume: '       210'
issue: '2'
keyword:
- Nuclear and High Energy Physics
- Biophysics
- Biochemistry
- Condensed Matter Physics
language:
- iso: eng
month: '06'
oa_version: None
page: 246-259
publication: Journal of Magnetic Resonance
publication_identifier:
  issn:
  - 1090-7807
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: Accurate measurement of one-bond H–X heteronuclear dipolar couplings in MAS
  solid-state NMR
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 210
year: '2011'
...
---
_id: '8482'
abstract:
- lang: eng
  text: The SOFAST-HMQC experiment [P. Schanda, B. Brutscher, Very fast two-dimensional
    NMR spectroscopy for real-time investigation of dynamic events in proteins on
    the time scale of seconds, J. Am. Chem. Soc. 127 (2005) 8014–8015] allows recording
    two-dimensional correlation spectra of macromolecules such as proteins in only
    a few seconds acquisition time. To achieve the highest possible sensitivity, SOFAST-HMQC
    experiments are preferably performed on high-field NMR spectrometers equipped
    with cryogenically cooled probes. The duty cycle of over 80% in fast-pulsing SOFAST-HMQC
    experiments, however, may cause problems when using a cryogenic probe. Here we
    introduce SE-IPAP-SOFAST-HMQC, a new pulse sequence that provides comparable sensitivity
    to standard SOFAST-HMQC, while avoiding heteronuclear decoupling during 1H detection,
    and thus significantly reducing the radiofrequency load of the probe during the
    experiment. The experiment is also attractive for fast and sensitive measurement
    of heteronuclear one-bond spin coupling constants.
article_processing_charge: No
article_type: letter_note
author:
- 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: Bernhard
  full_name: Brutscher, Bernhard
  last_name: Brutscher
citation:
  ama: Kern T, Schanda P, Brutscher B. Sensitivity-enhanced IPAP-SOFAST-HMQC for fast-pulsing
    2D NMR with reduced radiofrequency load. <i>Journal of Magnetic Resonance</i>.
    2008;190(2):333-338. doi:<a href="https://doi.org/10.1016/j.jmr.2007.11.015">10.1016/j.jmr.2007.11.015</a>
  apa: Kern, T., Schanda, P., &#38; Brutscher, B. (2008). Sensitivity-enhanced IPAP-SOFAST-HMQC
    for fast-pulsing 2D NMR with reduced radiofrequency load. <i>Journal of Magnetic
    Resonance</i>. Elsevier. <a href="https://doi.org/10.1016/j.jmr.2007.11.015">https://doi.org/10.1016/j.jmr.2007.11.015</a>
  chicago: Kern, Thomas, Paul Schanda, and Bernhard Brutscher. “Sensitivity-Enhanced
    IPAP-SOFAST-HMQC for Fast-Pulsing 2D NMR with Reduced Radiofrequency Load.” <i>Journal
    of Magnetic Resonance</i>. Elsevier, 2008. <a href="https://doi.org/10.1016/j.jmr.2007.11.015">https://doi.org/10.1016/j.jmr.2007.11.015</a>.
  ieee: T. Kern, P. Schanda, and B. Brutscher, “Sensitivity-enhanced IPAP-SOFAST-HMQC
    for fast-pulsing 2D NMR with reduced radiofrequency load,” <i>Journal of Magnetic
    Resonance</i>, vol. 190, no. 2. Elsevier, pp. 333–338, 2008.
  ista: Kern T, Schanda P, Brutscher B. 2008. Sensitivity-enhanced IPAP-SOFAST-HMQC
    for fast-pulsing 2D NMR with reduced radiofrequency load. Journal of Magnetic
    Resonance. 190(2), 333–338.
  mla: Kern, Thomas, et al. “Sensitivity-Enhanced IPAP-SOFAST-HMQC for Fast-Pulsing
    2D NMR with Reduced Radiofrequency Load.” <i>Journal of Magnetic Resonance</i>,
    vol. 190, no. 2, Elsevier, 2008, pp. 333–38, doi:<a href="https://doi.org/10.1016/j.jmr.2007.11.015">10.1016/j.jmr.2007.11.015</a>.
  short: T. Kern, P. Schanda, B. Brutscher, Journal of Magnetic Resonance 190 (2008)
    333–338.
date_created: 2020-09-18T10:12:46Z
date_published: 2008-02-01T00:00:00Z
date_updated: 2021-01-12T08:19:35Z
day: '01'
doi: 10.1016/j.jmr.2007.11.015
extern: '1'
intvolume: '       190'
issue: '2'
keyword:
- Nuclear and High Energy Physics
- Biophysics
- Biochemistry
- Condensed Matter Physics
language:
- iso: eng
month: '02'
oa_version: None
page: 333-338
publication: Journal of Magnetic Resonance
publication_identifier:
  issn:
  - 1090-7807
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: Sensitivity-enhanced IPAP-SOFAST-HMQC for fast-pulsing 2D NMR with reduced
  radiofrequency load
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 190
year: '2008'
...
---
_id: '8484'
abstract:
- lang: eng
  text: A series of sequential, intra-residue, and bi-directional BEST H–N–CA, H–N–CO,
    and H–N–CB pulse sequences is presented that extends the BEST concept introduced
    recently for fast multidimensional protein NMR [Schanda et al., J. Am. Chem. Soc.
    128 (2006) 9042] to the complete set of experiments required for sequential resonance
    assignment. We demonstrate for the protein ubiquitin that 3D BEST H–N–C correlation
    spectra can be recorded on a 600 MHz NMR spectrometer equipped with a cryogenic
    probe in only a few minutes of acquisition time with sufficient sensitivity to
    detect all expected cross peaks.
article_processing_charge: No
article_type: letter_note
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: Bernhard
  full_name: Brutscher, Bernhard
  last_name: Brutscher
citation:
  ama: Lescop E, Schanda P, Brutscher B. A set of BEST triple-resonance experiments
    for time-optimized protein resonance assignment. <i>Journal of Magnetic Resonance</i>.
    2007;187(1):163-169. doi:<a href="https://doi.org/10.1016/j.jmr.2007.04.002">10.1016/j.jmr.2007.04.002</a>
  apa: Lescop, E., Schanda, P., &#38; Brutscher, B. (2007). A set of BEST triple-resonance
    experiments for time-optimized protein resonance assignment. <i>Journal of Magnetic
    Resonance</i>. Elsevier. <a href="https://doi.org/10.1016/j.jmr.2007.04.002">https://doi.org/10.1016/j.jmr.2007.04.002</a>
  chicago: Lescop, Ewen, Paul Schanda, and Bernhard Brutscher. “A Set of BEST Triple-Resonance
    Experiments for Time-Optimized Protein Resonance Assignment.” <i>Journal of Magnetic
    Resonance</i>. Elsevier, 2007. <a href="https://doi.org/10.1016/j.jmr.2007.04.002">https://doi.org/10.1016/j.jmr.2007.04.002</a>.
  ieee: E. Lescop, P. Schanda, and B. Brutscher, “A set of BEST triple-resonance experiments
    for time-optimized protein resonance assignment,” <i>Journal of Magnetic Resonance</i>,
    vol. 187, no. 1. Elsevier, pp. 163–169, 2007.
  ista: Lescop E, Schanda P, Brutscher B. 2007. A set of BEST triple-resonance experiments
    for time-optimized protein resonance assignment. Journal of Magnetic Resonance.
    187(1), 163–169.
  mla: Lescop, Ewen, et al. “A Set of BEST Triple-Resonance Experiments for Time-Optimized
    Protein Resonance Assignment.” <i>Journal of Magnetic Resonance</i>, vol. 187,
    no. 1, Elsevier, 2007, pp. 163–69, doi:<a href="https://doi.org/10.1016/j.jmr.2007.04.002">10.1016/j.jmr.2007.04.002</a>.
  short: E. Lescop, P. Schanda, B. Brutscher, Journal of Magnetic Resonance 187 (2007)
    163–169.
date_created: 2020-09-18T10:13:02Z
date_published: 2007-07-01T00:00:00Z
date_updated: 2021-01-12T08:19:35Z
day: '01'
doi: 10.1016/j.jmr.2007.04.002
extern: '1'
intvolume: '       187'
issue: '1'
language:
- iso: eng
month: '07'
oa_version: None
page: 163-169
publication: Journal of Magnetic Resonance
publication_identifier:
  issn:
  - 1090-7807
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: A set of BEST triple-resonance experiments for time-optimized protein resonance
  assignment
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 187
year: '2007'
...
---
_id: '8490'
abstract:
- lang: eng
  text: We demonstrate the feasibility of recording 1H–15N correlation spectra of
    proteins in only one second of acquisition time. The experiment combines recently
    proposed SOFAST-HMQC with Hadamard-type 15N frequency encoding. This allows site-resolved
    real-time NMR studies of kinetic processes in proteins with an increased time
    resolution. The sensitivity of the experiment is sufficient to be applicable to
    a wide range of molecular systems available at millimolar concentration on a high
    magnetic field spectrometer.
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. Hadamard frequency-encoded SOFAST-HMQC for ultrafast
    two-dimensional protein NMR. <i>Journal of Magnetic Resonance</i>. 2006;178(2):334-339.
    doi:<a href="https://doi.org/10.1016/j.jmr.2005.10.007">10.1016/j.jmr.2005.10.007</a>
  apa: Schanda, P., &#38; Brutscher, B. (2006). Hadamard frequency-encoded SOFAST-HMQC
    for ultrafast two-dimensional protein NMR. <i>Journal of Magnetic Resonance</i>.
    Elsevier. <a href="https://doi.org/10.1016/j.jmr.2005.10.007">https://doi.org/10.1016/j.jmr.2005.10.007</a>
  chicago: Schanda, Paul, and Bernhard Brutscher. “Hadamard Frequency-Encoded SOFAST-HMQC
    for Ultrafast Two-Dimensional Protein NMR.” <i>Journal of Magnetic Resonance</i>.
    Elsevier, 2006. <a href="https://doi.org/10.1016/j.jmr.2005.10.007">https://doi.org/10.1016/j.jmr.2005.10.007</a>.
  ieee: P. Schanda and B. Brutscher, “Hadamard frequency-encoded SOFAST-HMQC for ultrafast
    two-dimensional protein NMR,” <i>Journal of Magnetic Resonance</i>, vol. 178,
    no. 2. Elsevier, pp. 334–339, 2006.
  ista: Schanda P, Brutscher B. 2006. Hadamard frequency-encoded SOFAST-HMQC for ultrafast
    two-dimensional protein NMR. Journal of Magnetic Resonance. 178(2), 334–339.
  mla: Schanda, Paul, and Bernhard Brutscher. “Hadamard Frequency-Encoded SOFAST-HMQC
    for Ultrafast Two-Dimensional Protein NMR.” <i>Journal of Magnetic Resonance</i>,
    vol. 178, no. 2, Elsevier, 2006, pp. 334–39, doi:<a href="https://doi.org/10.1016/j.jmr.2005.10.007">10.1016/j.jmr.2005.10.007</a>.
  short: P. Schanda, B. Brutscher, Journal of Magnetic Resonance 178 (2006) 334–339.
date_created: 2020-09-18T10:13:51Z
date_published: 2006-02-01T00:00:00Z
date_updated: 2021-01-12T08:19:38Z
day: '01'
doi: 10.1016/j.jmr.2005.10.007
extern: '1'
intvolume: '       178'
issue: '2'
keyword:
- Nuclear and High Energy Physics
- Biophysics
- Biochemistry
- Condensed Matter Physics
language:
- iso: eng
month: '02'
oa_version: None
page: 334-339
publication: Journal of Magnetic Resonance
publication_identifier:
  issn:
  - 1090-7807
publication_status: published
publisher: Elsevier
status: public
title: Hadamard frequency-encoded SOFAST-HMQC for ultrafast two-dimensional protein
  NMR
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 178
year: '2006'
...