---
_id: '14776'
abstract:
- lang: eng
  text: Soluble chaperones residing in the endoplasmic reticulum (ER) play vitally
    important roles in folding and quality control of newly synthesized proteins that
    transiently pass through the ER en route to their final destinations. These soluble
    residents of the ER are themselves endowed with an ER retrieval signal that enables
    the cell to bring the escaped residents back from the Golgi. Here, by using purified
    proteins, we showed that Nicotiana tabacum phytaspase, a plant aspartate-specific
    protease, introduces two breaks at the C-terminus of the N. tabacum ER resident
    calreticulin-3. These cleavages resulted in removal of either a dipeptide or a
    hexapeptide from the C-terminus of calreticulin-3 encompassing part or all of
    the ER retrieval signal. Consistently, expression of the calreticulin-3 derivative
    mimicking the phytaspase cleavage product in Nicotiana benthamiana cells demonstrated
    loss of the ER accumulation of the protein. Notably, upon its escape from the
    ER, calreticulin-3 was further processed by an unknown protease(s) to generate
    the free N-terminal (N) domain of calreticulin-3, which was ultimately secreted
    into the apoplast. Our study thus identified a specific proteolytic enzyme capable
    of precise detachment of the ER retrieval signal from a plant ER resident protein,
    with implications for the further fate of the escaped resident.
acknowledgement: "We thank C.U.T. Hellen for critically reading the manuscript. The
  MALDI MS facility and CLSM became available to us in the framework of Moscow State
  University Development Programs PNG 5.13 and PNR 5.13.\r\nThis work was funded by
  the Russian Science Foundation, grant numbers 19-14-00010 and 22-14-00071."
article_number: '16527'
article_processing_charge: Yes
article_type: original
author:
- first_name: Anastasiia
  full_name: Teplova, Anastasiia
  id: e3736151-106c-11ec-b916-c2558e2762c6
  last_name: Teplova
- first_name: Artemii A.
  full_name: Pigidanov, Artemii A.
  last_name: Pigidanov
- first_name: Marina V.
  full_name: Serebryakova, Marina V.
  last_name: Serebryakova
- first_name: Sergei A.
  full_name: Golyshev, Sergei A.
  last_name: Golyshev
- first_name: Raisa A.
  full_name: Galiullina, Raisa A.
  last_name: Galiullina
- first_name: Nina V.
  full_name: Chichkova, Nina V.
  last_name: Chichkova
- first_name: Andrey B.
  full_name: Vartapetian, Andrey B.
  last_name: Vartapetian
citation:
  ama: Teplova A, Pigidanov AA, Serebryakova MV, et al. Phytaspase Is capable of detaching
    the endoplasmic reticulum retrieval signal from tobacco calreticulin-3. <i>International
    Journal of Molecular Sciences</i>. 2023;24(22). doi:<a href="https://doi.org/10.3390/ijms242216527">10.3390/ijms242216527</a>
  apa: Teplova, A., Pigidanov, A. A., Serebryakova, M. V., Golyshev, S. A., Galiullina,
    R. A., Chichkova, N. V., &#38; Vartapetian, A. B. (2023). Phytaspase Is capable
    of detaching the endoplasmic reticulum retrieval signal from tobacco calreticulin-3.
    <i>International Journal of Molecular Sciences</i>. MDPI. <a href="https://doi.org/10.3390/ijms242216527">https://doi.org/10.3390/ijms242216527</a>
  chicago: Teplova, Anastasiia, Artemii A. Pigidanov, Marina V. Serebryakova, Sergei
    A. Golyshev, Raisa A. Galiullina, Nina V. Chichkova, and Andrey B. Vartapetian.
    “Phytaspase Is Capable of Detaching the Endoplasmic Reticulum Retrieval Signal
    from Tobacco Calreticulin-3.” <i>International Journal of Molecular Sciences</i>.
    MDPI, 2023. <a href="https://doi.org/10.3390/ijms242216527">https://doi.org/10.3390/ijms242216527</a>.
  ieee: A. Teplova <i>et al.</i>, “Phytaspase Is capable of detaching the endoplasmic
    reticulum retrieval signal from tobacco calreticulin-3,” <i>International Journal
    of Molecular Sciences</i>, vol. 24, no. 22. MDPI, 2023.
  ista: Teplova A, Pigidanov AA, Serebryakova MV, Golyshev SA, Galiullina RA, Chichkova
    NV, Vartapetian AB. 2023. Phytaspase Is capable of detaching the endoplasmic reticulum
    retrieval signal from tobacco calreticulin-3. International Journal of Molecular
    Sciences. 24(22), 16527.
  mla: Teplova, Anastasiia, et al. “Phytaspase Is Capable of Detaching the Endoplasmic
    Reticulum Retrieval Signal from Tobacco Calreticulin-3.” <i>International Journal
    of Molecular Sciences</i>, vol. 24, no. 22, 16527, MDPI, 2023, doi:<a href="https://doi.org/10.3390/ijms242216527">10.3390/ijms242216527</a>.
  short: A. Teplova, A.A. Pigidanov, M.V. Serebryakova, S.A. Golyshev, R.A. Galiullina,
    N.V. Chichkova, A.B. Vartapetian, International Journal of Molecular Sciences
    24 (2023).
date_created: 2024-01-10T09:24:35Z
date_published: 2023-11-01T00:00:00Z
date_updated: 2024-01-10T13:41:10Z
day: '01'
ddc:
- '580'
department:
- _id: JiFr
doi: 10.3390/ijms242216527
external_id:
  isi:
  - '001113792600001'
  pmid:
  - '38003717'
file:
- access_level: open_access
  checksum: 4df7d206ba022b7f54eff1f0aec1659a
  content_type: application/pdf
  creator: dernst
  date_created: 2024-01-10T13:39:42Z
  date_updated: 2024-01-10T13:39:42Z
  file_id: '14791'
  file_name: 2023_IJMS_Teplova.pdf
  file_size: 2637784
  relation: main_file
  success: 1
file_date_updated: 2024-01-10T13:39:42Z
has_accepted_license: '1'
intvolume: '        24'
isi: 1
issue: '22'
keyword:
- Inorganic Chemistry
- Organic Chemistry
- Physical and Theoretical Chemistry
- Computer Science Applications
- Spectroscopy
- Molecular Biology
- General Medicine
- Catalysis
language:
- iso: eng
month: '11'
oa: 1
oa_version: Published Version
pmid: 1
publication: International Journal of Molecular Sciences
publication_identifier:
  issn:
  - 1422-0067
publication_status: published
publisher: MDPI
quality_controlled: '1'
status: public
title: Phytaspase Is capable of detaching the endoplasmic reticulum retrieval signal
  from tobacco calreticulin-3
tmp:
  image: /images/cc_by.png
  legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
  name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
  short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 24
year: '2023'
...
---
_id: '11498'
abstract:
- lang: eng
  text: Rest-frame ultraviolet (UV) emission lines probe electron densities, gas-phase
    abundances, metallicities, and ionization parameters of the emitting star-forming
    galaxies and their environments. The strongest main UV emission line, Lyα, has
    been instrumental in advancing the general knowledge of galaxy formation in the
    early universe. However, observing Lyα emission becomes increasingly challenging
    at z ≳ 6 when the neutral hydrogen fraction of the circumgalactic and intergalactic
    media increases. Secondary weaker UV emission lines provide important alternative
    methods for studying galaxy properties at high redshift. We present a large sample
    of rest-frame UV emission line sources at intermediate redshift for calibrating
    and exploring the connection between secondary UV lines and the emitting galaxies’
    physical properties and their Lyα emission. The sample of 2052 emission line sources
    with 1.5 < z < 6.4 was collected from integral field data from the MUSE-Wide and
    MUSE-Deep surveys taken as part of Guaranteed Time Observations. The objects were
    selected through untargeted source detection (i.e., no preselection of sources
    as in dedicated spectroscopic campaigns) in the three-dimensional MUSE data cubes.
    We searched optimally extracted one-dimensional spectra of the full sample for
    UV emission features via emission line template matching, resulting in a sample
    of more than 100 rest-frame UV emission line detections. We show that the detection
    efficiency of (non-Lyα) UV emission lines increases with survey depth, and that
    the emission line strength of He IIλ1640 Å, [O III] λ1661 + O III] λ1666, and
    [Si III] λ1883 + Si III] λ1892 correlate with the strength of [C III] λ1907 +
    C III] λ1909. The rest-frame equivalent width (EW0) of [C III] λ1907 + C III]
    λ1909 is found to be roughly 0.22 ± 0.18 of EW0(Lyα). We measured the velocity
    offsets of resonant emission lines with respect to systemic tracers. For C IVλ1548
    + C IVλ1551 we find that ΔvC IV ≲ 250 km s−1, whereas ΔvLyα falls in the range
    of 250−500 km s−1 which is in agreement with previous results from the literature.
    The electron density ne measured from [Si III] λ1883 + Si III] λ1892 and [C III]
    λ1907 + C III] λ1909 line flux ratios is generally < 105 cm−3 and the gas-phase
    abundance is below solar at 12 + log10(O/H)≈8. Lastly, we used “PhotoIonization
    Model Probability Density Functions” to infer physical parameters of the full
    sample and individual systems based on photoionization model parameter grids and
    observational constraints from our UV emission line searches. This reveals that
    the UV line emitters generally have ionization parameter log10(U) ≈ −2.5 and metal
    mass fractions that scatter around Z ≈ 10−2, that is Z ≈ 0.66 Z⊙. Value-added
    catalogs of the full sample of MUSE objects studied in this work and a collection
    of UV line emitters from the literature are provided with this paper.
acknowledgement: 'We would like to thank Charlotte Mason for useful discussions and
  for providing the data for the curves shown in Fig. 13 and Dawn Erb for providing
  the observational data for the comparison sample studied by Steidel et al. (2014),
  also shown in Fig. 13. This work has been supported by the BMBF grant 05A14BAC and
  we acknowledge support by the Competitive Fund of the Leibniz Association through
  grant SAW-2015-AIP-2. AF acknowledges the support from grant PRIN MIUR2017-20173ML3WW_001.
  JS acknowledges the support from Vici grant 639.043.409 from the Dutch Research
  Council (NWO). GM received funding from the European Union’s Horizon 2020 research
  and innovation programme under the Marie Sklodowska-Curie grant agreement No MARACAS
  – DLV-896778. This paper is based on observations collected at the European Organisation
  for Astronomical Research in the Southern Hemisphere under ESO programmes 094.A-0289(B),
  095.A-0010(A), 096.A-0045(A), 096.A-0045(B), 094.A-0205, 095.A-0240, 096.A-0090,
  097.A-0160, and 098.A-0017. This paper also makes use of observations made with
  the NASA/ESA Hubble Space Telescope obtained at STScI. This research made use of
  the following programs and open-source packages for Python and we are thankful to
  their developers: DS9 (Joye & Mandel 2003), Astropy (Astropy Collaboration 2013,
  2018), APLpy (Robitaille & Bressert 2012), iPython (Pérez & Granger 2007), numpy
  (van der Walt et al. 2011), matplotlib (Hunter 2007), and SciPy (Jones et al. 2001).'
article_number: A80
article_processing_charge: No
article_type: original
arxiv: 1
author:
- first_name: K. B.
  full_name: Schmidt, K. B.
  last_name: Schmidt
- first_name: J.
  full_name: Kerutt, J.
  last_name: Kerutt
- first_name: L.
  full_name: Wisotzki, L.
  last_name: Wisotzki
- first_name: T.
  full_name: Urrutia, T.
  last_name: Urrutia
- first_name: A.
  full_name: Feltre, A.
  last_name: Feltre
- first_name: M. V.
  full_name: Maseda, M. V.
  last_name: Maseda
- first_name: T.
  full_name: Nanayakkara, T.
  last_name: Nanayakkara
- first_name: R.
  full_name: Bacon, R.
  last_name: Bacon
- first_name: L. A.
  full_name: Boogaard, L. A.
  last_name: Boogaard
- first_name: S.
  full_name: Conseil, S.
  last_name: Conseil
- first_name: T.
  full_name: Contini, T.
  last_name: Contini
- first_name: E. C.
  full_name: Herenz, E. C.
  last_name: Herenz
- first_name: W.
  full_name: Kollatschny, W.
  last_name: Kollatschny
- first_name: M.
  full_name: Krumpe, M.
  last_name: Krumpe
- first_name: F.
  full_name: Leclercq, F.
  last_name: Leclercq
- first_name: G.
  full_name: Mahler, G.
  last_name: Mahler
- first_name: Jorryt J
  full_name: Matthee, Jorryt J
  id: 7439a258-f3c0-11ec-9501-9df22fe06720
  last_name: Matthee
  orcid: 0000-0003-2871-127X
- first_name: V.
  full_name: Mauerhofer, V.
  last_name: Mauerhofer
- first_name: J.
  full_name: Richard, J.
  last_name: Richard
- first_name: J.
  full_name: Schaye, J.
  last_name: Schaye
citation:
  ama: Schmidt KB, Kerutt J, Wisotzki L, et al. Recovery and analysis of rest-frame
    UV emission lines in 2052 galaxies observed with MUSE at 1.5 &#60; z &#60; 6.4.
    <i>Astronomy &#38; Astrophysics</i>. 2021;654. doi:<a href="https://doi.org/10.1051/0004-6361/202140876">10.1051/0004-6361/202140876</a>
  apa: Schmidt, K. B., Kerutt, J., Wisotzki, L., Urrutia, T., Feltre, A., Maseda,
    M. V., … Schaye, J. (2021). Recovery and analysis of rest-frame UV emission lines
    in 2052 galaxies observed with MUSE at 1.5 &#60; z &#60; 6.4. <i>Astronomy &#38;
    Astrophysics</i>. EDP Sciences. <a href="https://doi.org/10.1051/0004-6361/202140876">https://doi.org/10.1051/0004-6361/202140876</a>
  chicago: Schmidt, K. B., J. Kerutt, L. Wisotzki, T. Urrutia, A. Feltre, M. V. Maseda,
    T. Nanayakkara, et al. “Recovery and Analysis of Rest-Frame UV Emission Lines
    in 2052 Galaxies Observed with MUSE at 1.5 &#60; z &#60; 6.4.” <i>Astronomy &#38;
    Astrophysics</i>. EDP Sciences, 2021. <a href="https://doi.org/10.1051/0004-6361/202140876">https://doi.org/10.1051/0004-6361/202140876</a>.
  ieee: K. B. Schmidt <i>et al.</i>, “Recovery and analysis of rest-frame UV emission
    lines in 2052 galaxies observed with MUSE at 1.5 &#60; z &#60; 6.4,” <i>Astronomy
    &#38; Astrophysics</i>, vol. 654. EDP Sciences, 2021.
  ista: Schmidt KB, Kerutt J, Wisotzki L, Urrutia T, Feltre A, Maseda MV, Nanayakkara
    T, Bacon R, Boogaard LA, Conseil S, Contini T, Herenz EC, Kollatschny W, Krumpe
    M, Leclercq F, Mahler G, Matthee JJ, Mauerhofer V, Richard J, Schaye J. 2021.
    Recovery and analysis of rest-frame UV emission lines in 2052 galaxies observed
    with MUSE at 1.5 &#60; z &#60; 6.4. Astronomy &#38; Astrophysics. 654, A80.
  mla: Schmidt, K. B., et al. “Recovery and Analysis of Rest-Frame UV Emission Lines
    in 2052 Galaxies Observed with MUSE at 1.5 &#60; z &#60; 6.4.” <i>Astronomy &#38;
    Astrophysics</i>, vol. 654, A80, EDP Sciences, 2021, doi:<a href="https://doi.org/10.1051/0004-6361/202140876">10.1051/0004-6361/202140876</a>.
  short: K.B. Schmidt, J. Kerutt, L. Wisotzki, T. Urrutia, A. Feltre, M.V. Maseda,
    T. Nanayakkara, R. Bacon, L.A. Boogaard, S. Conseil, T. Contini, E.C. Herenz,
    W. Kollatschny, M. Krumpe, F. Leclercq, G. Mahler, J.J. Matthee, V. Mauerhofer,
    J. Richard, J. Schaye, Astronomy &#38; Astrophysics 654 (2021).
date_created: 2022-07-06T08:49:03Z
date_published: 2021-10-15T00:00:00Z
date_updated: 2022-07-19T09:34:36Z
day: '15'
doi: 10.1051/0004-6361/202140876
extern: '1'
external_id:
  arxiv:
  - '2108.01713'
intvolume: '       654'
keyword:
- Space and Planetary Science
- Astronomy and Astrophysics
- 'ultraviolet: galaxies / galaxies: high-redshift / galaxies: ISM / ISM: lines and
  bands / methods: observational / techniques: imaging spectroscopy'
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://arxiv.org/abs/2108.01713
month: '10'
oa: 1
oa_version: Published Version
publication: Astronomy & Astrophysics
publication_identifier:
  eissn:
  - 1432-0746
  issn:
  - 0004-6361
publication_status: published
publisher: EDP Sciences
quality_controlled: '1'
scopus_import: '1'
status: public
title: Recovery and analysis of rest-frame UV emission lines in 2052 galaxies observed
  with MUSE at 1.5 < z < 6.4
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 654
year: '2021'
...
---
_id: '11526'
abstract:
- lang: eng
  text: We present the results from a MUSE survey of twelve z ≃ 3.15 quasars, which
    were selected to be much fainter (20 < iSDSS < 23) than in previous studies of
    giant Ly α nebulae around the brightest quasars (16.6 < iAB < 18.7). We detect
    H I Ly α nebulae around 100 per cent of our target quasars, with emission extending
    to scales of at least 60 physical kpc, and up to 190 pkpc. We explore correlations
    between properties of the nebulae and their host quasars, with the goal of connecting
    variations in the properties of the illuminating QSO to the response in nebular
    emission. We show that the surface brightness profiles of the nebulae are similar
    to those of nebulae around bright quasars, but with a lower normalization. Our
    targeted quasars are on average 3.7 mag (≃30 times) fainter in UV continuum than
    our bright reference sample, and yet the nebulae around them are only 4.3 times
    fainter in mean Ly α surface brightness, measured between 20 and 50 pkpc. We find
    significant correlations between the surface brightness of the nebula and the
    luminosity of the quasar in both UV continuum and Ly α. The latter can be interpreted
    as evidence for a substantial contribution from unresolved inner parts of the
    nebulae to the narrow components seen in the Ly α lines of some of our faint quasars,
    possibly from the inner circumgalactic medium or from the host galaxy’s interstellar
    medium.
acknowledgement: The authors thank Daichi Kashino, for providing access to unpublished
  zCOSMOS Deep data, and Jakob S. den Brok for sharing code used in den Brok et al.
  (2020). GP and SC acknowledge the support of the Swiss National Science Foundation
  [grant PP00P2163824]. SM is supported by the Experienced Researchers Fellowship,
  Alexander von Humboldt-Stiftung, Germany. This work is based on observations collected
  at the European Organisation for Astronomical Research in the Southern Hemisphere
  under the MUSE GTO programme. The major analysis and production of figures in this
  work was conducted in Python, using standard libraries which include NumPy (Harris
  et al. 2020), SciPy (Virtanen et al. 2020), Matplotlib (Hunter 2007) and the interactive
  command shell IPython (Pérez & Granger 2007). This research also made use of Astropy,
  a community-developed core Python package for Astronomy (Astropy Collaboration et
  al. 2013), and Photutils, an Astropy package for detection and photometry of astronomica
  sources (Bradley et al. 2019). The python interface dustmaps (Green 2018) was used
  to query galactic extinction maps. topcat, a graphical tool for manipulating tabular
  data, was also utilized in this analysis (Taylor 2005). This research has made use
  of the "Aladin sky atlas" developed at CDS, Strasbourg Observatory, France (Bonnarel
  et al. 2000).
article_processing_charge: No
article_type: original
arxiv: 1
author:
- first_name: Ruari
  full_name: Mackenzie, Ruari
  last_name: Mackenzie
- first_name: Gabriele
  full_name: Pezzulli, Gabriele
  last_name: Pezzulli
- first_name: Sebastiano
  full_name: Cantalupo, Sebastiano
  last_name: Cantalupo
- first_name: Raffaella A
  full_name: Marino, Raffaella A
  last_name: Marino
- first_name: Simon
  full_name: Lilly, Simon
  last_name: Lilly
- first_name: Sowgat
  full_name: Muzahid, Sowgat
  last_name: Muzahid
- first_name: Jorryt J
  full_name: Matthee, Jorryt J
  id: 7439a258-f3c0-11ec-9501-9df22fe06720
  last_name: Matthee
  orcid: 0000-0003-2871-127X
- first_name: Joop
  full_name: Schaye, Joop
  last_name: Schaye
- first_name: Lutz
  full_name: Wisotzki, Lutz
  last_name: Wisotzki
citation:
  ama: Mackenzie R, Pezzulli G, Cantalupo S, et al. Revealing the impact of quasar
    luminosity on giant Lyα nebulae. <i>Monthly Notices of the Royal Astronomical
    Society</i>. 2021;502(1):494-509. doi:<a href="https://doi.org/10.1093/mnras/staa3277">10.1093/mnras/staa3277</a>
  apa: Mackenzie, R., Pezzulli, G., Cantalupo, S., Marino, R. A., Lilly, S., Muzahid,
    S., … Wisotzki, L. (2021). Revealing the impact of quasar luminosity on giant
    Lyα nebulae. <i>Monthly Notices of the Royal Astronomical Society</i>. Oxford
    University Press. <a href="https://doi.org/10.1093/mnras/staa3277">https://doi.org/10.1093/mnras/staa3277</a>
  chicago: Mackenzie, Ruari, Gabriele Pezzulli, Sebastiano Cantalupo, Raffaella A
    Marino, Simon Lilly, Sowgat Muzahid, Jorryt J Matthee, Joop Schaye, and Lutz Wisotzki.
    “Revealing the Impact of Quasar Luminosity on Giant Lyα Nebulae.” <i>Monthly Notices
    of the Royal Astronomical Society</i>. Oxford University Press, 2021. <a href="https://doi.org/10.1093/mnras/staa3277">https://doi.org/10.1093/mnras/staa3277</a>.
  ieee: R. Mackenzie <i>et al.</i>, “Revealing the impact of quasar luminosity on
    giant Lyα nebulae,” <i>Monthly Notices of the Royal Astronomical Society</i>,
    vol. 502, no. 1. Oxford University Press, pp. 494–509, 2021.
  ista: Mackenzie R, Pezzulli G, Cantalupo S, Marino RA, Lilly S, Muzahid S, Matthee
    JJ, Schaye J, Wisotzki L. 2021. Revealing the impact of quasar luminosity on giant
    Lyα nebulae. Monthly Notices of the Royal Astronomical Society. 502(1), 494–509.
  mla: Mackenzie, Ruari, et al. “Revealing the Impact of Quasar Luminosity on Giant
    Lyα Nebulae.” <i>Monthly Notices of the Royal Astronomical Society</i>, vol. 502,
    no. 1, Oxford University Press, 2021, pp. 494–509, doi:<a href="https://doi.org/10.1093/mnras/staa3277">10.1093/mnras/staa3277</a>.
  short: R. Mackenzie, G. Pezzulli, S. Cantalupo, R.A. Marino, S. Lilly, S. Muzahid,
    J.J. Matthee, J. Schaye, L. Wisotzki, Monthly Notices of the Royal Astronomical
    Society 502 (2021) 494–509.
date_created: 2022-07-07T10:11:15Z
date_published: 2021-03-01T00:00:00Z
date_updated: 2022-08-18T10:56:28Z
day: '01'
doi: 10.1093/mnras/staa3277
extern: '1'
external_id:
  arxiv:
  - '2010.12589'
intvolume: '       502'
issue: '1'
keyword:
- Space and Planetary Science
- Astronomy and Astrophysics
- 'techniques: imaging spectroscopy'
- intergalactic medium
- 'quasars: emission lines'
- 'quasars: general'
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://arxiv.org/abs/2010.12589
month: '03'
oa: 1
oa_version: Preprint
page: 494-509
publication: Monthly Notices of the Royal Astronomical Society
publication_identifier:
  eissn:
  - 1365-2966
  issn:
  - 0035-8711
publication_status: published
publisher: Oxford University Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: Revealing the impact of quasar luminosity on giant Lyα nebulae
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 502
year: '2021'
...
---
_id: '13386'
abstract:
- lang: eng
  text: Azobenzenealkanethiols in self-assembled monolayers (SAMs) on Au(111) exhibit
    reversible trans–cis photoisomerization when diluted with alkanethiol spacers.
    Using these mixed SAMs, we show switching of the linear optical and second-harmonic
    response. The effective switching of these surface optical properties relies on
    a reasonably large cross section and a high photoisomerization yield as well as
    a long lifetime of the metastable cis isomer. We quantified the switching process
    by X-ray absorption spectroscopy. The cross sections for the trans–cis and cis–trans
    photoisomerization with 365 and 455 nm light, respectively, are 1 order of magnitude
    smaller than in solution. In vacuum, the 365 nm photostationary state comprises
    50–74% of the molecules in the cis form, limited by their rapid thermal isomerization
    back to the trans state. In contrast, the 455 nm photostationary state contains
    nearly 100% trans-azobenzene. We determined time constants for the thermal cis–trans
    isomerization of only a few minutes in vacuum and in a dry nitrogen atmosphere
    but of more than 1 day in ambient air. Our results suggest that adventitious water
    adsorbed on the surface of the SAM stabilizes the polar cis configuration of azobenzene
    under ambient conditions. The back reaction rate constants differing by 2 orders
    of magnitude underline the huge influence of the environment and, accordingly,
    its importance when comparing various experiments.
article_processing_charge: No
article_type: original
author:
- first_name: Thomas
  full_name: Moldt, Thomas
  last_name: Moldt
- first_name: Daniel
  full_name: Przyrembel, Daniel
  last_name: Przyrembel
- first_name: Michael
  full_name: Schulze, Michael
  last_name: Schulze
- first_name: Wibke
  full_name: Bronsch, Wibke
  last_name: Bronsch
- first_name: Larissa
  full_name: Boie, Larissa
  last_name: Boie
- first_name: Daniel
  full_name: Brete, Daniel
  last_name: Brete
- first_name: Cornelius
  full_name: Gahl, Cornelius
  last_name: Gahl
- first_name: Rafal
  full_name: Klajn, Rafal
  id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b
  last_name: Klajn
- first_name: Petra
  full_name: Tegeder, Petra
  last_name: Tegeder
- first_name: Martin
  full_name: Weinelt, Martin
  last_name: Weinelt
citation:
  ama: Moldt T, Przyrembel D, Schulze M, et al. Differing isomerization kinetics of
    azobenzene-functionalized self-assembled monolayers in ambient air and in vacuum.
    <i>Langmuir</i>. 2016;32(42):10795-10801. doi:<a href="https://doi.org/10.1021/acs.langmuir.6b01690">10.1021/acs.langmuir.6b01690</a>
  apa: Moldt, T., Przyrembel, D., Schulze, M., Bronsch, W., Boie, L., Brete, D., …
    Weinelt, M. (2016). Differing isomerization kinetics of azobenzene-functionalized
    self-assembled monolayers in ambient air and in vacuum. <i>Langmuir</i>. American
    Chemical Society. <a href="https://doi.org/10.1021/acs.langmuir.6b01690">https://doi.org/10.1021/acs.langmuir.6b01690</a>
  chicago: Moldt, Thomas, Daniel Przyrembel, Michael Schulze, Wibke Bronsch, Larissa
    Boie, Daniel Brete, Cornelius Gahl, Rafal Klajn, Petra Tegeder, and Martin Weinelt.
    “Differing Isomerization Kinetics of Azobenzene-Functionalized Self-Assembled
    Monolayers in Ambient Air and in Vacuum.” <i>Langmuir</i>. American Chemical Society,
    2016. <a href="https://doi.org/10.1021/acs.langmuir.6b01690">https://doi.org/10.1021/acs.langmuir.6b01690</a>.
  ieee: T. Moldt <i>et al.</i>, “Differing isomerization kinetics of azobenzene-functionalized
    self-assembled monolayers in ambient air and in vacuum,” <i>Langmuir</i>, vol.
    32, no. 42. American Chemical Society, pp. 10795–10801, 2016.
  ista: Moldt T, Przyrembel D, Schulze M, Bronsch W, Boie L, Brete D, Gahl C, Klajn
    R, Tegeder P, Weinelt M. 2016. Differing isomerization kinetics of azobenzene-functionalized
    self-assembled monolayers in ambient air and in vacuum. Langmuir. 32(42), 10795–10801.
  mla: Moldt, Thomas, et al. “Differing Isomerization Kinetics of Azobenzene-Functionalized
    Self-Assembled Monolayers in Ambient Air and in Vacuum.” <i>Langmuir</i>, vol.
    32, no. 42, American Chemical Society, 2016, pp. 10795–801, doi:<a href="https://doi.org/10.1021/acs.langmuir.6b01690">10.1021/acs.langmuir.6b01690</a>.
  short: T. Moldt, D. Przyrembel, M. Schulze, W. Bronsch, L. Boie, D. Brete, C. Gahl,
    R. Klajn, P. Tegeder, M. Weinelt, Langmuir 32 (2016) 10795–10801.
date_created: 2023-08-01T09:42:37Z
date_published: 2016-10-25T00:00:00Z
date_updated: 2023-08-07T12:27:06Z
day: '25'
doi: 10.1021/acs.langmuir.6b01690
extern: '1'
external_id:
  pmid:
  - '27681851'
intvolume: '        32'
issue: '42'
keyword:
- Electrochemistry
- Spectroscopy
- Surfaces and Interfaces
- Condensed Matter Physics
- General Materials Science
language:
- iso: eng
month: '10'
oa_version: None
page: 10795-10801
pmid: 1
publication: Langmuir
publication_identifier:
  eissn:
  - 1520-5827
  issn:
  - 0743-7463
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Differing isomerization kinetics of azobenzene-functionalized self-assembled
  monolayers in ambient air and in vacuum
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 32
year: '2016'
...
---
_id: '13396'
abstract:
- lang: eng
  text: 'Photoswitching in densely packed azobenzene self-assembled monolayers (SAMs)
    is strongly affected by steric constraints and excitonic coupling between neighboring
    chromophores. Therefore, control of the chromophore density is essential for enhancing
    and manipulating the photoisomerization yield. We systematically compare two methods
    to achieve this goal: First, we assemble monocomponent azobenzene–alkanethiolate
    SAMs on gold nanoparticles of varying size. Second, we form mixed SAMs of azobenzene–alkanethiolates
    and “dummy” alkanethiolates on planar substrates. Both methods lead to a gradual
    decrease of the chromophore density and enable efficient photoswitching with low-power
    light sources. X-ray spectroscopy reveals that coadsorption from solution yields
    mixtures with tunable composition. The orientation of the chromophores with respect
    to the surface normal changes from a tilted to an upright position with increasing
    azobenzene density. For both systems, optical spectroscopy reveals a pronounced
    excitonic shift that increases with the chromophore density. In spite of exciting
    the optical transition of the monomer, the main spectral change in mixed SAMs
    occurs in the excitonic band. In addition, the photoisomerization yield decreases
    only slightly by increasing the azobenzene–alkanethiolate density, and we observed
    photoswitching even with minor dilutions. Unlike in solution, azobenzene in the
    planar SAM can be switched back almost completely by optical excitation from the
    cis to the original trans state within a short time scale. These observations
    indicate cooperativity in the photoswitching process of mixed SAMs.'
article_processing_charge: No
article_type: original
author:
- first_name: Thomas
  full_name: Moldt, Thomas
  last_name: Moldt
- first_name: Daniel
  full_name: Brete, Daniel
  last_name: Brete
- first_name: Daniel
  full_name: Przyrembel, Daniel
  last_name: Przyrembel
- first_name: Sanjib
  full_name: Das, Sanjib
  last_name: Das
- first_name: Joel R.
  full_name: Goldman, Joel R.
  last_name: Goldman
- first_name: Pintu K.
  full_name: Kundu, Pintu K.
  last_name: Kundu
- first_name: Cornelius
  full_name: Gahl, Cornelius
  last_name: Gahl
- first_name: Rafal
  full_name: Klajn, Rafal
  id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b
  last_name: Klajn
- first_name: Martin
  full_name: Weinelt, Martin
  last_name: Weinelt
citation:
  ama: Moldt T, Brete D, Przyrembel D, et al. Tailoring the properties of surface-immobilized
    azobenzenes by monolayer dilution and surface curvature. <i>Langmuir</i>. 2015;31(3):1048-1057.
    doi:<a href="https://doi.org/10.1021/la504291n">10.1021/la504291n</a>
  apa: Moldt, T., Brete, D., Przyrembel, D., Das, S., Goldman, J. R., Kundu, P. K.,
    … Weinelt, M. (2015). Tailoring the properties of surface-immobilized azobenzenes
    by monolayer dilution and surface curvature. <i>Langmuir</i>. American Chemical
    Society. <a href="https://doi.org/10.1021/la504291n">https://doi.org/10.1021/la504291n</a>
  chicago: Moldt, Thomas, Daniel Brete, Daniel Przyrembel, Sanjib Das, Joel R. Goldman,
    Pintu K. Kundu, Cornelius Gahl, Rafal Klajn, and Martin Weinelt. “Tailoring the
    Properties of Surface-Immobilized Azobenzenes by Monolayer Dilution and Surface
    Curvature.” <i>Langmuir</i>. American Chemical Society, 2015. <a href="https://doi.org/10.1021/la504291n">https://doi.org/10.1021/la504291n</a>.
  ieee: T. Moldt <i>et al.</i>, “Tailoring the properties of surface-immobilized azobenzenes
    by monolayer dilution and surface curvature,” <i>Langmuir</i>, vol. 31, no. 3.
    American Chemical Society, pp. 1048–1057, 2015.
  ista: Moldt T, Brete D, Przyrembel D, Das S, Goldman JR, Kundu PK, Gahl C, Klajn
    R, Weinelt M. 2015. Tailoring the properties of surface-immobilized azobenzenes
    by monolayer dilution and surface curvature. Langmuir. 31(3), 1048–1057.
  mla: Moldt, Thomas, et al. “Tailoring the Properties of Surface-Immobilized Azobenzenes
    by Monolayer Dilution and Surface Curvature.” <i>Langmuir</i>, vol. 31, no. 3,
    American Chemical Society, 2015, pp. 1048–57, doi:<a href="https://doi.org/10.1021/la504291n">10.1021/la504291n</a>.
  short: T. Moldt, D. Brete, D. Przyrembel, S. Das, J.R. Goldman, P.K. Kundu, C. Gahl,
    R. Klajn, M. Weinelt, Langmuir 31 (2015) 1048–1057.
date_created: 2023-08-01T09:45:02Z
date_published: 2015-01-27T00:00:00Z
date_updated: 2023-08-07T13:05:04Z
day: '27'
doi: 10.1021/la504291n
extern: '1'
external_id:
  pmid:
  - '25544061'
intvolume: '        31'
issue: '3'
keyword:
- Electrochemistry
- Spectroscopy
- Surfaces and Interfaces
- Condensed Matter Physics
- General Materials Science
language:
- iso: eng
month: '01'
oa_version: None
page: 1048-1057
pmid: 1
publication: Langmuir
publication_identifier:
  eissn:
  - 1520-5827
  issn:
  - 0743-7463
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Tailoring the properties of surface-immobilized azobenzenes by monolayer dilution
  and surface curvature
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 31
year: '2015'
...
---
_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. <i>Journal of Biomolecular
    NMR</i>. 2013;57(3):263-280. doi:<a href="https://doi.org/10.1007/s10858-013-9787-x">10.1007/s10858-013-9787-x</a>'
  apa: 'Haller, J. D., &#38; 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. <i>Journal of Biomolecular
    NMR</i>. Springer Nature. <a href="https://doi.org/10.1007/s10858-013-9787-x">https://doi.org/10.1007/s10858-013-9787-x</a>'
  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.” <i>Journal of Biomolecular
    NMR</i>. Springer Nature, 2013. <a href="https://doi.org/10.1007/s10858-013-9787-x">https://doi.org/10.1007/s10858-013-9787-x</a>.'
  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,” <i>Journal of Biomolecular
    NMR</i>, 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.” <i>Journal of Biomolecular
    NMR</i>, vol. 57, no. 3, Springer Nature, 2013, pp. 263–80, doi:<a href="https://doi.org/10.1007/s10858-013-9787-x">10.1007/s10858-013-9787-x</a>.'
  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: '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. <i>Journal of Biomolecular NMR</i>. 2009;43:1-10. doi:<a href="https://doi.org/10.1007/s10858-008-9284-9">10.1007/s10858-008-9284-9</a>'
  apa: 'Gal, M., Kern, T., Schanda, P., Frydman, L., &#38; Brutscher, B. (2009). An
    improved ultrafast 2D NMR experiment: Towards atom-resolved real-time studies
    of protein kinetics at multi-Hz rates. <i>Journal of Biomolecular NMR</i>. Springer
    Nature. <a href="https://doi.org/10.1007/s10858-008-9284-9">https://doi.org/10.1007/s10858-008-9284-9</a>'
  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.” <i>Journal of Biomolecular NMR</i>. Springer
    Nature, 2009. <a href="https://doi.org/10.1007/s10858-008-9284-9">https://doi.org/10.1007/s10858-008-9284-9</a>.'
  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,” <i>Journal of Biomolecular NMR</i>, 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.” <i>Journal of Biomolecular
    NMR</i>, vol. 43, Springer Nature, 2009, pp. 1–10, doi:<a href="https://doi.org/10.1007/s10858-008-9284-9">10.1007/s10858-008-9284-9</a>.'
  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.
    <i>Journal of Biomolecular NMR</i>. 2007;38:47-55. doi:<a href="https://doi.org/10.1007/s10858-006-9138-2">10.1007/s10858-006-9138-2</a>
  apa: Schanda, P., Lescop, E., Falge, M., Sounier, R., Boisbouvier, J., &#38; Brutscher,
    B. (2007). Sensitivity-optimized experiment for the measurement of residual dipolar
    couplings between amide protons. <i>Journal of Biomolecular NMR</i>. Springer
    Nature. <a href="https://doi.org/10.1007/s10858-006-9138-2">https://doi.org/10.1007/s10858-006-9138-2</a>
  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.” <i>Journal of Biomolecular
    NMR</i>. Springer Nature, 2007. <a href="https://doi.org/10.1007/s10858-006-9138-2">https://doi.org/10.1007/s10858-006-9138-2</a>.
  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,” <i>Journal of Biomolecular NMR</i>, 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.” <i>Journal of Biomolecular
    NMR</i>, vol. 38, Springer Nature, 2007, pp. 47–55, doi:<a href="https://doi.org/10.1007/s10858-006-9138-2">10.1007/s10858-006-9138-2</a>.
  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: '13426'
abstract:
- lang: eng
  text: Photoswelling of thin films of dichromated gelatin provides a basis for fabrication
    of multilevel surface reliefs via sequential UV illumination through different
    photomasks. The remarkable feature of this simple, benchtop technique is that
    by adjusting irradiation times, film thickness, or its hydration state the heights
    of the developed features can be varied from few nanometers to tens of microns.
    After UV exposure, the surface structures can be replicated faithfully into either
    soft or hard PDMS stamps.
article_processing_charge: No
article_type: original
author:
- first_name: Maciej
  full_name: Paszewski, Maciej
  last_name: Paszewski
- 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: Paszewski M, Smoukov SK, Klajn R, Grzybowski BA. Multilevel surface nano- and
    microstructuring via sequential photoswelling of dichromated gelatin. <i>Langmuir</i>.
    2007;23(10):5419-5422. doi:<a href="https://doi.org/10.1021/la062982c">10.1021/la062982c</a>
  apa: Paszewski, M., Smoukov, S. K., Klajn, R., &#38; Grzybowski, B. A. (2007). Multilevel
    surface nano- and microstructuring via sequential photoswelling of dichromated
    gelatin. <i>Langmuir</i>. American Chemical Society. <a href="https://doi.org/10.1021/la062982c">https://doi.org/10.1021/la062982c</a>
  chicago: Paszewski, Maciej, Stoyan K. Smoukov, Rafal Klajn, and Bartosz A. Grzybowski.
    “Multilevel Surface Nano- and Microstructuring via Sequential Photoswelling of
    Dichromated Gelatin.” <i>Langmuir</i>. American Chemical Society, 2007. <a href="https://doi.org/10.1021/la062982c">https://doi.org/10.1021/la062982c</a>.
  ieee: M. Paszewski, S. K. Smoukov, R. Klajn, and B. A. Grzybowski, “Multilevel surface
    nano- and microstructuring via sequential photoswelling of dichromated gelatin,”
    <i>Langmuir</i>, vol. 23, no. 10. American Chemical Society, pp. 5419–5422, 2007.
  ista: Paszewski M, Smoukov SK, Klajn R, Grzybowski BA. 2007. Multilevel surface
    nano- and microstructuring via sequential photoswelling of dichromated gelatin.
    Langmuir. 23(10), 5419–5422.
  mla: Paszewski, Maciej, et al. “Multilevel Surface Nano- and Microstructuring via
    Sequential Photoswelling of Dichromated Gelatin.” <i>Langmuir</i>, vol. 23, no.
    10, American Chemical Society, 2007, pp. 5419–22, doi:<a href="https://doi.org/10.1021/la062982c">10.1021/la062982c</a>.
  short: M. Paszewski, S.K. Smoukov, R. Klajn, B.A. Grzybowski, Langmuir 23 (2007)
    5419–5422.
date_created: 2023-08-01T10:31:33Z
date_published: 2007-04-11T00:00:00Z
date_updated: 2023-08-08T11:26:24Z
day: '11'
doi: 10.1021/la062982c
extern: '1'
external_id:
  pmid:
  - '17425340'
intvolume: '        23'
issue: '10'
keyword:
- Electrochemistry
- Spectroscopy
- Surfaces and Interfaces
- Condensed Matter Physics
- General Materials Science
language:
- iso: eng
month: '04'
oa_version: None
page: 5419-5422
pmid: 1
publication: Langmuir
publication_identifier:
  eissn:
  - 1520-5827
  issn:
  - 0743-7463
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Multilevel surface nano- and microstructuring via sequential photoswelling
  of dichromated gelatin
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 23
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. <i>Journal
    of Biomolecular NMR</i>. 2005;33(4):199-211. doi:<a href="https://doi.org/10.1007/s10858-005-4425-x">10.1007/s10858-005-4425-x</a>
  apa: Schanda, P., Kupče, Ē., &#38; Brutscher, B. (2005). SOFAST-HMQC experiments
    for recording two-dimensional deteronuclear correlation spectra of proteins within
    a few seconds. <i>Journal of Biomolecular NMR</i>. Springer Nature. <a href="https://doi.org/10.1007/s10858-005-4425-x">https://doi.org/10.1007/s10858-005-4425-x</a>
  chicago: Schanda, Paul, Ēriks Kupče, and Bernhard Brutscher. “SOFAST-HMQC Experiments
    for Recording Two-Dimensional Deteronuclear Correlation Spectra of Proteins within
    a Few Seconds.” <i>Journal of Biomolecular NMR</i>. Springer Nature, 2005. <a
    href="https://doi.org/10.1007/s10858-005-4425-x">https://doi.org/10.1007/s10858-005-4425-x</a>.
  ieee: P. Schanda, Ē. Kupče, and B. Brutscher, “SOFAST-HMQC experiments for recording
    two-dimensional deteronuclear correlation spectra of proteins within a few seconds,”
    <i>Journal of Biomolecular NMR</i>, 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.” <i>Journal
    of Biomolecular NMR</i>, vol. 33, no. 4, Springer Nature, 2005, pp. 199–211, doi:<a
    href="https://doi.org/10.1007/s10858-005-4425-x">10.1007/s10858-005-4425-x</a>.
  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'
...
---
_id: '13432'
abstract:
- lang: eng
  text: A new experimental technique is described that uses reaction−diffusion phenomena
    as a means of one-step microfabrication of complex, multilevel surface reliefs.
    Thin films of dry gelatin doped with potassium hexacyanoferrate are chemically
    micropatterned with a solution of silver nitrate delivered from an agarose stamp.
    Precipitation reaction between the two salts causes the surface to deform. The
    mechanism of surface deformation is shown to involve a sequence of reactions,
    diffusion, and gel swelling/contraction. This mechanism is established experimentally
    and provides a basis of a theoretical lattice-gas model that allows prediction
    surface topographies emerging from arbitrary geometries of the stamped features.
    The usefulness of the technique is demonstrated by using it to rapidly prepare
    two types of mold for passive microfluidic mixers.
article_processing_charge: No
article_type: original
author:
- first_name: Christopher J.
  full_name: Campbell, Christopher J.
  last_name: Campbell
- first_name: Rafal
  full_name: Klajn, Rafal
  id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b
  last_name: Klajn
- first_name: Marcin
  full_name: Fialkowski, Marcin
  last_name: Fialkowski
- first_name: Bartosz A.
  full_name: Grzybowski, Bartosz A.
  last_name: Grzybowski
citation:
  ama: Campbell CJ, Klajn R, Fialkowski M, Grzybowski BA. One-step multilevel microfabrication
    by reaction−diffusion. <i>Langmuir</i>. 2005;21(1):418-423. doi:<a href="https://doi.org/10.1021/la0487747">10.1021/la0487747</a>
  apa: Campbell, C. J., Klajn, R., Fialkowski, M., &#38; Grzybowski, B. A. (2005).
    One-step multilevel microfabrication by reaction−diffusion. <i>Langmuir</i>. American
    Chemical Society. <a href="https://doi.org/10.1021/la0487747">https://doi.org/10.1021/la0487747</a>
  chicago: Campbell, Christopher J., Rafal Klajn, Marcin Fialkowski, and Bartosz A.
    Grzybowski. “One-Step Multilevel Microfabrication by Reaction−diffusion.” <i>Langmuir</i>.
    American Chemical Society, 2005. <a href="https://doi.org/10.1021/la0487747">https://doi.org/10.1021/la0487747</a>.
  ieee: C. J. Campbell, R. Klajn, M. Fialkowski, and B. A. Grzybowski, “One-step multilevel
    microfabrication by reaction−diffusion,” <i>Langmuir</i>, vol. 21, no. 1. American
    Chemical Society, pp. 418–423, 2005.
  ista: Campbell CJ, Klajn R, Fialkowski M, Grzybowski BA. 2005. One-step multilevel
    microfabrication by reaction−diffusion. Langmuir. 21(1), 418–423.
  mla: Campbell, Christopher J., et al. “One-Step Multilevel Microfabrication by Reaction−diffusion.”
    <i>Langmuir</i>, vol. 21, no. 1, American Chemical Society, 2005, pp. 418–23,
    doi:<a href="https://doi.org/10.1021/la0487747">10.1021/la0487747</a>.
  short: C.J. Campbell, R. Klajn, M. Fialkowski, B.A. Grzybowski, Langmuir 21 (2005)
    418–423.
date_created: 2023-08-01T10:38:29Z
date_published: 2005-01-21T00:00:00Z
date_updated: 2023-08-08T12:15:48Z
day: '21'
doi: 10.1021/la0487747
extern: '1'
external_id:
  pmid:
  - '15620333'
intvolume: '        21'
issue: '1'
keyword:
- Electrochemistry
- Spectroscopy
- Surfaces and Interfaces
- Condensed Matter Physics
- General Materials Science
language:
- iso: eng
month: '01'
oa_version: None
page: 418-423
pmid: 1
publication: Langmuir
publication_identifier:
  eissn:
  - 1520-5827
  issn:
  - 0743-7463
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: One-step multilevel microfabrication by reaction−diffusion
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 21
year: '2005'
...