---
_id: '8410'
article_processing_charge: No
article_type: letter_note
author:
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Eduard Y.
full_name: Chekmenev, Eduard Y.
last_name: Chekmenev
citation:
ama: Schanda P, Chekmenev EY. NMR for Biological Systems. ChemPhysChem. 2019;20(2):177-177.
doi:10.1002/cphc.201801100
apa: Schanda, P., & Chekmenev, E. Y. (2019). NMR for Biological Systems. ChemPhysChem.
Wiley. https://doi.org/10.1002/cphc.201801100
chicago: Schanda, Paul, and Eduard Y. Chekmenev. “NMR for Biological Systems.” ChemPhysChem.
Wiley, 2019. https://doi.org/10.1002/cphc.201801100.
ieee: P. Schanda and E. Y. Chekmenev, “NMR for Biological Systems,” ChemPhysChem,
vol. 20, no. 2. Wiley, pp. 177–177, 2019.
ista: Schanda P, Chekmenev EY. 2019. NMR for Biological Systems. ChemPhysChem. 20(2),
177–177.
mla: Schanda, Paul, and Eduard Y. Chekmenev. “NMR for Biological Systems.” ChemPhysChem,
vol. 20, no. 2, Wiley, 2019, pp. 177–177, doi:10.1002/cphc.201801100.
short: P. Schanda, E.Y. Chekmenev, ChemPhysChem 20 (2019) 177–177.
date_created: 2020-09-17T10:29:26Z
date_published: 2019-01-21T00:00:00Z
date_updated: 2021-01-12T08:19:05Z
day: '21'
doi: 10.1002/cphc.201801100
extern: '1'
external_id:
pmid:
- '30556633'
intvolume: ' 20'
issue: '2'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1002/cphc.201801100
month: '01'
oa: 1
oa_version: Published Version
page: 177-177
pmid: 1
publication: ChemPhysChem
publication_identifier:
issn:
- 1439-4235
publication_status: published
publisher: Wiley
quality_controlled: '1'
status: public
title: NMR for Biological Systems
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 20
year: '2019'
...
---
_id: '8411'
abstract:
- lang: eng
text: 'Studying protein dynamics on microsecond‐to‐millisecond (μs‐ms) time scales
can provide important insight into protein function. In magic‐angle‐spinning (MAS)
NMR, μs dynamics can be visualized by R1p rotating‐frame relaxation dispersion
experiments in different regimes of radio‐frequency field strengths: at low RF
field strength, isotropic‐chemical‐shift fluctuation leads to “Bloch‐McConnell‐type”
relaxation dispersion, while when the RF field approaches rotary resonance conditions
bond angle fluctuations manifest as increased R1p rate constants (“Near‐Rotary‐Resonance
Relaxation Dispersion”, NERRD). Here we explore the joint analysis of both regimes
to gain comprehensive insight into motion in terms of geometric amplitudes, chemical‐shift
changes, populations and exchange kinetics. We use a numerical simulation procedure
to illustrate these effects and the potential of extracting exchange parameters,
and apply the methodology to the study of a previously described conformational
exchange process in microcrystalline ubiquitin.'
article_processing_charge: No
article_type: original
author:
- first_name: Dominique
full_name: Marion, Dominique
last_name: Marion
- first_name: Diego F.
full_name: Gauto, Diego F.
last_name: Gauto
- first_name: Isabel
full_name: Ayala, Isabel
last_name: Ayala
- first_name: Karine
full_name: Giandoreggio-Barranco, Karine
last_name: Giandoreggio-Barranco
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: Marion D, Gauto DF, Ayala I, Giandoreggio-Barranco K, Schanda P. Microsecond
protein dynamics from combined Bloch-McConnell and Near-Rotary-Resonance R1p relaxation-dispersion
MAS NMR. ChemPhysChem. 2019;20(2):276-284. doi:10.1002/cphc.201800935
apa: Marion, D., Gauto, D. F., Ayala, I., Giandoreggio-Barranco, K., & Schanda,
P. (2019). Microsecond protein dynamics from combined Bloch-McConnell and Near-Rotary-Resonance
R1p relaxation-dispersion MAS NMR. ChemPhysChem. Wiley. https://doi.org/10.1002/cphc.201800935
chicago: Marion, Dominique, Diego F. Gauto, Isabel Ayala, Karine Giandoreggio-Barranco,
and Paul Schanda. “Microsecond Protein Dynamics from Combined Bloch-McConnell
and Near-Rotary-Resonance R1p Relaxation-Dispersion MAS NMR.” ChemPhysChem.
Wiley, 2019. https://doi.org/10.1002/cphc.201800935.
ieee: D. Marion, D. F. Gauto, I. Ayala, K. Giandoreggio-Barranco, and P. Schanda,
“Microsecond protein dynamics from combined Bloch-McConnell and Near-Rotary-Resonance
R1p relaxation-dispersion MAS NMR,” ChemPhysChem, vol. 20, no. 2. Wiley,
pp. 276–284, 2019.
ista: Marion D, Gauto DF, Ayala I, Giandoreggio-Barranco K, Schanda P. 2019. Microsecond
protein dynamics from combined Bloch-McConnell and Near-Rotary-Resonance R1p relaxation-dispersion
MAS NMR. ChemPhysChem. 20(2), 276–284.
mla: Marion, Dominique, et al. “Microsecond Protein Dynamics from Combined Bloch-McConnell
and Near-Rotary-Resonance R1p Relaxation-Dispersion MAS NMR.” ChemPhysChem,
vol. 20, no. 2, Wiley, 2019, pp. 276–84, doi:10.1002/cphc.201800935.
short: D. Marion, D.F. Gauto, I. Ayala, K. Giandoreggio-Barranco, P. Schanda, ChemPhysChem
20 (2019) 276–284.
date_created: 2020-09-17T10:29:36Z
date_published: 2019-01-21T00:00:00Z
date_updated: 2021-01-12T08:19:06Z
day: '21'
doi: 10.1002/cphc.201800935
extern: '1'
external_id:
pmid:
- '30444575'
intvolume: ' 20'
issue: '2'
keyword:
- Physical and Theoretical Chemistry
- Atomic and Molecular Physics
- and Optics
language:
- iso: eng
month: '01'
oa_version: Submitted Version
page: 276-284
pmid: 1
publication: ChemPhysChem
publication_identifier:
issn:
- 1439-4235
publication_status: published
publisher: Wiley
quality_controlled: '1'
status: public
title: Microsecond protein dynamics from combined Bloch-McConnell and Near-Rotary-Resonance
R1p relaxation-dispersion MAS NMR
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 20
year: '2019'
...
---
_id: '8412'
abstract:
- lang: eng
text: Microsecond to millisecond timescale backbone dynamics of the amyloid core
residues in Y145Stop human prion protein (PrP) fibrils were investigated by using
15N rotating frame (R1ρ) relaxation dispersion solid‐state nuclear magnetic resonance
spectroscopy over a wide range of spin‐lock fields. Numerical simulations enabled
the experimental relaxation dispersion profiles for most of the fibril core residues
to be modelled by using a two‐state exchange process with a common exchange rate
of 1000 s−1, corresponding to protein backbone motion on the timescale of 1 ms,
and an excited‐state population of 2 %. We also found that the relaxation dispersion
profiles for several amino acids positioned near the edges of the most structured
regions of the amyloid core were better modelled by assuming somewhat higher excited‐state
populations (∼5–15 %) and faster exchange rate constants, corresponding to protein
backbone motions on the timescale of ∼100–300 μs. The slow backbone dynamics of
the core residues were evaluated in the context of the structural model of human
Y145Stop PrP amyloid.
article_processing_charge: No
article_type: original
author:
- first_name: Matthew D.
full_name: Shannon, Matthew D.
last_name: Shannon
- first_name: Theint
full_name: Theint, Theint
last_name: Theint
- first_name: Dwaipayan
full_name: Mukhopadhyay, Dwaipayan
last_name: Mukhopadhyay
- first_name: Krystyna
full_name: Surewicz, Krystyna
last_name: Surewicz
- first_name: Witold K.
full_name: Surewicz, Witold K.
last_name: Surewicz
- first_name: Dominique
full_name: Marion, Dominique
last_name: Marion
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Christopher P.
full_name: Jaroniec, Christopher P.
last_name: Jaroniec
citation:
ama: Shannon MD, Theint T, Mukhopadhyay D, et al. Conformational dynamics in the
core of human Y145Stop prion protein amyloid probed by relaxation dispersion NMR.
ChemPhysChem. 2019;20(2):311-317. doi:10.1002/cphc.201800779
apa: Shannon, M. D., Theint, T., Mukhopadhyay, D., Surewicz, K., Surewicz, W. K.,
Marion, D., … Jaroniec, C. P. (2019). Conformational dynamics in the core of human
Y145Stop prion protein amyloid probed by relaxation dispersion NMR. ChemPhysChem.
Wiley. https://doi.org/10.1002/cphc.201800779
chicago: Shannon, Matthew D., Theint Theint, Dwaipayan Mukhopadhyay, Krystyna Surewicz,
Witold K. Surewicz, Dominique Marion, Paul Schanda, and Christopher P. Jaroniec.
“Conformational Dynamics in the Core of Human Y145Stop Prion Protein Amyloid Probed
by Relaxation Dispersion NMR.” ChemPhysChem. Wiley, 2019. https://doi.org/10.1002/cphc.201800779.
ieee: M. D. Shannon et al., “Conformational dynamics in the core of human
Y145Stop prion protein amyloid probed by relaxation dispersion NMR,” ChemPhysChem,
vol. 20, no. 2. Wiley, pp. 311–317, 2019.
ista: Shannon MD, Theint T, Mukhopadhyay D, Surewicz K, Surewicz WK, Marion D, Schanda
P, Jaroniec CP. 2019. Conformational dynamics in the core of human Y145Stop prion
protein amyloid probed by relaxation dispersion NMR. ChemPhysChem. 20(2), 311–317.
mla: Shannon, Matthew D., et al. “Conformational Dynamics in the Core of Human Y145Stop
Prion Protein Amyloid Probed by Relaxation Dispersion NMR.” ChemPhysChem,
vol. 20, no. 2, Wiley, 2019, pp. 311–17, doi:10.1002/cphc.201800779.
short: M.D. Shannon, T. Theint, D. Mukhopadhyay, K. Surewicz, W.K. Surewicz, D.
Marion, P. Schanda, C.P. Jaroniec, ChemPhysChem 20 (2019) 311–317.
date_created: 2020-09-17T10:29:43Z
date_published: 2019-01-21T00:00:00Z
date_updated: 2021-01-12T08:19:06Z
day: '21'
doi: 10.1002/cphc.201800779
extern: '1'
external_id:
pmid:
- '30276945'
intvolume: ' 20'
issue: '2'
keyword:
- Physical and Theoretical Chemistry
- Atomic and Molecular Physics
- and Optics
language:
- iso: eng
month: '01'
oa_version: Submitted Version
page: 311-317
pmid: 1
publication: ChemPhysChem
publication_identifier:
issn:
- 1439-4235
publication_status: published
publisher: Wiley
quality_controlled: '1'
status: public
title: Conformational dynamics in the core of human Y145Stop prion protein amyloid
probed by relaxation dispersion NMR
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 20
year: '2019'
...
---
_id: '8446'
abstract:
- lang: eng
text: Solid‐state NMR spectroscopy can provide insight into protein structure and
dynamics at the atomic level without inherent protein size limitations. However,
a major hurdle to studying large proteins by solid‐state NMR spectroscopy is related
to spectral complexity and resonance overlap, which increase with molecular weight
and severely hamper the assignment process. Here the use of two sets of experiments
is shown to expand the tool kit of 1H‐detected assignment approaches, which correlate
a given amide pair either to the two adjacent CO–CA pairs (4D hCOCANH/hCOCAcoNH),
or to the amide 1H of the neighboring residue (3D HcocaNH/HcacoNH, which can be
extended to 5D). The experiments are based on efficient coherence transfers between
backbone atoms using INEPT transfers between carbons and cross‐polarization for
heteronuclear transfers. The utility of these experiments is exemplified with
application to assemblies of deuterated, fully amide‐protonated proteins from
approximately 20 to 60 kDa monomer, at magic‐angle spinning (MAS) frequencies
from approximately 40 to 55 kHz. These experiments will also be applicable to
protonated proteins at higher MAS frequencies. The resonance assignment of a domain
within the 50.4 kDa bacteriophage T5 tube protein pb6 is reported, and this is
compared to NMR assignments of the isolated domain in solution. This comparison
reveals contacts of this domain to the core of the polymeric tail tube assembly.
article_processing_charge: No
article_type: original
author:
- first_name: Hugo
full_name: Fraga, Hugo
last_name: Fraga
- first_name: Charles‐Adrien
full_name: Arnaud, Charles‐Adrien
last_name: Arnaud
- first_name: Diego F.
full_name: Gauto, Diego F.
last_name: Gauto
- first_name: Maxime
full_name: Audin, Maxime
last_name: Audin
- first_name: Vilius
full_name: Kurauskas, Vilius
last_name: Kurauskas
- first_name: Pavel
full_name: Macek, Pavel
last_name: Macek
- first_name: Carsten
full_name: Krichel, Carsten
last_name: Krichel
- first_name: Jia‐Ying
full_name: Guan, Jia‐Ying
last_name: Guan
- first_name: Jerome
full_name: Boisbouvier, Jerome
last_name: Boisbouvier
- first_name: Remco
full_name: Sprangers, Remco
last_name: Sprangers
- first_name: Cécile
full_name: Breyton, Cécile
last_name: Breyton
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: Fraga H, Arnaud C, Gauto DF, et al. Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D
correlation experiments for resonance assignment of large proteins. ChemPhysChem.
2017;18(19):2697-2703. doi:10.1002/cphc.201700572
apa: Fraga, H., Arnaud, C., Gauto, D. F., Audin, M., Kurauskas, V., Macek, P., …
Schanda, P. (2017). Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D correlation experiments
for resonance assignment of large proteins. ChemPhysChem. Wiley. https://doi.org/10.1002/cphc.201700572
chicago: Fraga, Hugo, Charles‐Adrien Arnaud, Diego F. Gauto, Maxime Audin, Vilius
Kurauskas, Pavel Macek, Carsten Krichel, et al. “Solid‐state NMR H–N–(C)–H and
H–N–C–C 3D/4D Correlation Experiments for Resonance Assignment of Large Proteins.”
ChemPhysChem. Wiley, 2017. https://doi.org/10.1002/cphc.201700572.
ieee: H. Fraga et al., “Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D correlation
experiments for resonance assignment of large proteins,” ChemPhysChem,
vol. 18, no. 19. Wiley, pp. 2697–2703, 2017.
ista: Fraga H, Arnaud C, Gauto DF, Audin M, Kurauskas V, Macek P, Krichel C, Guan
J, Boisbouvier J, Sprangers R, Breyton C, Schanda P. 2017. Solid‐state NMR H–N–(C)–H
and H–N–C–C 3D/4D correlation experiments for resonance assignment of large proteins.
ChemPhysChem. 18(19), 2697–2703.
mla: Fraga, Hugo, et al. “Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D Correlation
Experiments for Resonance Assignment of Large Proteins.” ChemPhysChem,
vol. 18, no. 19, Wiley, 2017, pp. 2697–703, doi:10.1002/cphc.201700572.
short: H. Fraga, C. Arnaud, D.F. Gauto, M. Audin, V. Kurauskas, P. Macek, C. Krichel,
J. Guan, J. Boisbouvier, R. Sprangers, C. Breyton, P. Schanda, ChemPhysChem 18
(2017) 2697–2703.
date_created: 2020-09-18T10:06:09Z
date_published: 2017-08-09T00:00:00Z
date_updated: 2021-01-12T08:19:19Z
day: '09'
doi: 10.1002/cphc.201700572
extern: '1'
intvolume: ' 18'
issue: '19'
keyword:
- Physical and Theoretical Chemistry
- Atomic and Molecular Physics
- and Optics
language:
- iso: eng
month: '08'
oa_version: None
page: 2697-2703
publication: ChemPhysChem
publication_identifier:
issn:
- 1439-4235
- 1439-7641
publication_status: published
publisher: Wiley
quality_controlled: '1'
status: public
title: Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D correlation experiments for resonance
assignment of large proteins
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 18
year: '2017'
...
---
_id: '13388'
abstract:
- lang: eng
text: The Inside Cover picture illustrates the fluorescent properties of a gold
nanocluster functionalized with several copies of a red-emitting merocyanine (image
by Ella Marushchenko). The red fluorescence can be turned on and off reversibly
by using an external stimulus.
article_processing_charge: No
author:
- first_name: T.
full_name: Udayabhaskararao, T.
last_name: Udayabhaskararao
- first_name: Pintu K.
full_name: Kundu, Pintu K.
last_name: Kundu
- first_name: Johannes
full_name: Ahrens, Johannes
last_name: Ahrens
- first_name: Rafal
full_name: Klajn, Rafal
id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b
last_name: Klajn
citation:
ama: 'Udayabhaskararao T, Kundu PK, Ahrens J, Klajn R. Inside Cover: Reversible
Photoisomerization of Spiropyran on the Surfaces of Au25 Nanoclusters (ChemPhysChem
12/2016). Vol 17. Wiley; 2016:1711-1711. doi:10.1002/cphc.201600480'
apa: 'Udayabhaskararao, T., Kundu, P. K., Ahrens, J., & Klajn, R. (2016). Inside
cover: Reversible photoisomerization of spiropyran on the surfaces of Au25 nanoclusters
(ChemPhysChem 12/2016). ChemPhysChem (Vol. 17, pp. 1711–1711). Wiley.
https://doi.org/10.1002/cphc.201600480'
chicago: 'Udayabhaskararao, T., Pintu K. Kundu, Johannes Ahrens, and Rafal Klajn.
Inside Cover: Reversible Photoisomerization of Spiropyran on the Surfaces of
Au25 Nanoclusters (ChemPhysChem 12/2016). ChemPhysChem. Vol. 17. Wiley,
2016. https://doi.org/10.1002/cphc.201600480.'
ieee: 'T. Udayabhaskararao, P. K. Kundu, J. Ahrens, and R. Klajn, Inside cover:
Reversible photoisomerization of spiropyran on the surfaces of Au25 nanoclusters
(ChemPhysChem 12/2016), vol. 17, no. 12. Wiley, 2016, pp. 1711–1711.'
ista: 'Udayabhaskararao T, Kundu PK, Ahrens J, Klajn R. 2016. Inside cover: Reversible
photoisomerization of spiropyran on the surfaces of Au25 nanoclusters (ChemPhysChem
12/2016), Wiley,p.'
mla: 'Udayabhaskararao, T., et al. “Inside Cover: Reversible Photoisomerization
of Spiropyran on the Surfaces of Au25 Nanoclusters (ChemPhysChem 12/2016).” ChemPhysChem,
vol. 17, no. 12, Wiley, 2016, pp. 1711–1711, doi:10.1002/cphc.201600480.'
short: 'T. Udayabhaskararao, P.K. Kundu, J. Ahrens, R. Klajn, Inside Cover: Reversible
Photoisomerization of Spiropyran on the Surfaces of Au25 Nanoclusters (ChemPhysChem
12/2016), Wiley, 2016.'
date_created: 2023-08-01T09:43:07Z
date_published: 2016-06-17T00:00:00Z
date_updated: 2023-08-07T12:43:38Z
day: '17'
doi: 10.1002/cphc.201600480
extern: '1'
intvolume: ' 17'
issue: '12'
keyword:
- Physical and Theoretical Chemistry
- Atomic and Molecular Physics
- and Optics
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1002/cphc.201600480
month: '06'
oa: 1
oa_version: Published Version
page: 1711-1711
publication: ChemPhysChem
publication_identifier:
eissn:
- 1439-7641
issn:
- 1439-4235
publication_status: published
publisher: Wiley
quality_controlled: '1'
status: public
title: 'Inside cover: Reversible photoisomerization of spiropyran on the surfaces
of Au25 nanoclusters (ChemPhysChem 12/2016)'
type: other_academic_publication
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 17
year: '2016'
...
---
_id: '13389'
abstract:
- lang: eng
text: Au25 nanoclusters functionalized with a spiropyran molecular switch are synthesized
via a ligand-exchange reaction at low temperature. The resulting nanoclusters
are characterized by optical and NMR spectroscopies as well as by mass spectrometry.
Spiropyran bound to nanoclusters isomerizes in a reversible fashion when exposed
to UV and visible light, and its properties are similar to those of free spiropyran
molecules in solution. The reversible photoisomerization entails the modulation
of fluorescence as well as the light-controlled self-assembly of nanoclusters.
article_processing_charge: No
article_type: original
author:
- first_name: T.
full_name: Udayabhaskararao, T.
last_name: Udayabhaskararao
- first_name: Pintu K.
full_name: Kundu, Pintu K.
last_name: Kundu
- first_name: Johannes
full_name: Ahrens, Johannes
last_name: Ahrens
- first_name: Rafal
full_name: Klajn, Rafal
id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b
last_name: Klajn
citation:
ama: Udayabhaskararao T, Kundu PK, Ahrens J, Klajn R. Reversible photoisomerization
of spiropyran on the surfaces of Au25 nanoclusters. ChemPhysChem. 2016;17(12):1805-1809.
doi:10.1002/cphc.201500897
apa: Udayabhaskararao, T., Kundu, P. K., Ahrens, J., & Klajn, R. (2016). Reversible
photoisomerization of spiropyran on the surfaces of Au25 nanoclusters. ChemPhysChem.
Wiley. https://doi.org/10.1002/cphc.201500897
chicago: Udayabhaskararao, T., Pintu K. Kundu, Johannes Ahrens, and Rafal Klajn.
“Reversible Photoisomerization of Spiropyran on the Surfaces of Au25 Nanoclusters.”
ChemPhysChem. Wiley, 2016. https://doi.org/10.1002/cphc.201500897.
ieee: T. Udayabhaskararao, P. K. Kundu, J. Ahrens, and R. Klajn, “Reversible photoisomerization
of spiropyran on the surfaces of Au25 nanoclusters,” ChemPhysChem, vol.
17, no. 12. Wiley, pp. 1805–1809, 2016.
ista: Udayabhaskararao T, Kundu PK, Ahrens J, Klajn R. 2016. Reversible photoisomerization
of spiropyran on the surfaces of Au25 nanoclusters. ChemPhysChem. 17(12), 1805–1809.
mla: Udayabhaskararao, T., et al. “Reversible Photoisomerization of Spiropyran on
the Surfaces of Au25 Nanoclusters.” ChemPhysChem, vol. 17, no. 12, Wiley,
2016, pp. 1805–09, doi:10.1002/cphc.201500897.
short: T. Udayabhaskararao, P.K. Kundu, J. Ahrens, R. Klajn, ChemPhysChem 17 (2016)
1805–1809.
date_created: 2023-08-01T09:43:18Z
date_published: 2016-06-17T00:00:00Z
date_updated: 2023-08-07T12:46:46Z
day: '17'
doi: 10.1002/cphc.201500897
extern: '1'
external_id:
pmid:
- '26593975'
intvolume: ' 17'
issue: '12'
keyword:
- Physical and Theoretical Chemistry
- Atomic and Molecular Physics
- and Optics
language:
- iso: eng
month: '06'
oa_version: None
page: 1805-1809
pmid: 1
publication: ChemPhysChem
publication_identifier:
eissn:
- 1439-7641
issn:
- 1439-4235
publication_status: published
publisher: Wiley
quality_controlled: '1'
scopus_import: '1'
status: public
title: Reversible photoisomerization of spiropyran on the surfaces of Au25 nanoclusters
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 17
year: '2016'
...
---
_id: '8470'
abstract:
- lang: eng
text: 'Adding a new dimension: 4D or 3D proton‐detected spectra of perdeuterated
protein samples with 1H labelled amides and methyl groups permit collecting unambiguous
distance restraints with high sensitivity and determining protein structure by
solid‐state NMR (see picture).'
article_processing_charge: No
article_type: original
author:
- first_name: Matthias
full_name: Huber, Matthias
last_name: Huber
- first_name: Sebastian
full_name: Hiller, Sebastian
last_name: Hiller
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Matthias
full_name: Ernst, Matthias
last_name: Ernst
- first_name: Anja
full_name: Böckmann, Anja
last_name: Böckmann
- first_name: René
full_name: Verel, René
last_name: Verel
- first_name: Beat H.
full_name: Meier, Beat H.
last_name: Meier
citation:
ama: Huber M, Hiller S, Schanda P, et al. A proton-detected 4D solid-state NMR experiment
for protein structure determination. ChemPhysChem. 2011;12(5):915-918.
doi:10.1002/cphc.201100062
apa: Huber, M., Hiller, S., Schanda, P., Ernst, M., Böckmann, A., Verel, R., &
Meier, B. H. (2011). A proton-detected 4D solid-state NMR experiment for protein
structure determination. ChemPhysChem. Wiley. https://doi.org/10.1002/cphc.201100062
chicago: Huber, Matthias, Sebastian Hiller, Paul Schanda, Matthias Ernst, Anja Böckmann,
René Verel, and Beat H. Meier. “A Proton-Detected 4D Solid-State NMR Experiment
for Protein Structure Determination.” ChemPhysChem. Wiley, 2011. https://doi.org/10.1002/cphc.201100062.
ieee: M. Huber et al., “A proton-detected 4D solid-state NMR experiment for
protein structure determination,” ChemPhysChem, vol. 12, no. 5. Wiley,
pp. 915–918, 2011.
ista: Huber M, Hiller S, Schanda P, Ernst M, Böckmann A, Verel R, Meier BH. 2011.
A proton-detected 4D solid-state NMR experiment for protein structure determination.
ChemPhysChem. 12(5), 915–918.
mla: Huber, Matthias, et al. “A Proton-Detected 4D Solid-State NMR Experiment for
Protein Structure Determination.” ChemPhysChem, vol. 12, no. 5, Wiley,
2011, pp. 915–18, doi:10.1002/cphc.201100062.
short: M. Huber, S. Hiller, P. Schanda, M. Ernst, A. Böckmann, R. Verel, B.H. Meier,
ChemPhysChem 12 (2011) 915–918.
date_created: 2020-09-18T10:10:56Z
date_published: 2011-02-15T00:00:00Z
date_updated: 2021-01-12T08:19:30Z
day: '15'
doi: 10.1002/cphc.201100062
extern: '1'
intvolume: ' 12'
issue: '5'
keyword:
- Physical and Theoretical Chemistry
- Atomic and Molecular Physics
- and Optics
language:
- iso: eng
month: '02'
oa_version: None
page: 915-918
publication: ChemPhysChem
publication_identifier:
issn:
- 1439-4235
publication_status: published
publisher: Wiley
quality_controlled: '1'
status: public
title: A proton-detected 4D solid-state NMR experiment for protein structure determination
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 12
year: '2011'
...