---
_id: '8443'
abstract:
- lang: eng
text: Characterizing the structure of membrane proteins (MPs) generally requires
extraction from their native environment, most commonly with detergents. Yet,
the physicochemical properties of detergent micelles and lipid bilayers differ
markedly and could alter the structural organization of MPs, albeit without general
rules. Dodecylphosphocholine (DPC) is the most widely used detergent for MP structure
determination by NMR, but the physiological relevance of several prominent structures
has been questioned, though indirectly, by other biophysical techniques, e.g.,
functional/thermostability assay (TSA) and molecular dynamics (MD) simulations.
Here, we resolve unambiguously this controversy by probing the functional relevance
of three different mitochondrial carriers (MCs) in DPC at the atomic level, using
an exhaustive set of solution-NMR experiments, complemented by functional/TSA
and MD data. Our results provide atomic-level insight into the structure, substrate
interaction and dynamics of the detergent–membrane protein complexes and demonstrates
cogently that, while high-resolution NMR signals can be obtained for MCs in DPC,
they systematically correspond to nonfunctional states.
article_processing_charge: No
article_type: original
author:
- first_name: Vilius
full_name: Kurauskas, Vilius
last_name: Kurauskas
- first_name: Audrey
full_name: Hessel, Audrey
last_name: Hessel
- first_name: Peixiang
full_name: Ma, Peixiang
last_name: Ma
- first_name: Paola
full_name: Lunetti, Paola
last_name: Lunetti
- first_name: Katharina
full_name: Weinhäupl, Katharina
last_name: Weinhäupl
- first_name: Lionel
full_name: Imbert, Lionel
last_name: Imbert
- first_name: Bernhard
full_name: Brutscher, Bernhard
last_name: Brutscher
- first_name: Martin S.
full_name: King, Martin S.
last_name: King
- first_name: Rémy
full_name: Sounier, Rémy
last_name: Sounier
- first_name: Vincenza
full_name: Dolce, Vincenza
last_name: Dolce
- first_name: Edmund R. S.
full_name: Kunji, Edmund R. S.
last_name: Kunji
- first_name: Loredana
full_name: Capobianco, Loredana
last_name: Capobianco
- first_name: Christophe
full_name: Chipot, Christophe
last_name: Chipot
- first_name: François
full_name: Dehez, François
last_name: Dehez
- first_name: Beate
full_name: Bersch, Beate
last_name: Bersch
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: 'Kurauskas V, Hessel A, Ma P, et al. How detergent impacts membrane proteins:
Atomic-level views of mitochondrial carriers in dodecylphosphocholine. The
Journal of Physical Chemistry Letters. 2018;9(5):933-938. doi:10.1021/acs.jpclett.8b00269'
apa: 'Kurauskas, V., Hessel, A., Ma, P., Lunetti, P., Weinhäupl, K., Imbert, L.,
… Schanda, P. (2018). How detergent impacts membrane proteins: Atomic-level views
of mitochondrial carriers in dodecylphosphocholine. The Journal of Physical
Chemistry Letters. American Chemical Society. https://doi.org/10.1021/acs.jpclett.8b00269'
chicago: 'Kurauskas, Vilius, Audrey Hessel, Peixiang Ma, Paola Lunetti, Katharina
Weinhäupl, Lionel Imbert, Bernhard Brutscher, et al. “How Detergent Impacts Membrane
Proteins: Atomic-Level Views of Mitochondrial Carriers in Dodecylphosphocholine.”
The Journal of Physical Chemistry Letters. American Chemical Society, 2018.
https://doi.org/10.1021/acs.jpclett.8b00269.'
ieee: 'V. Kurauskas et al., “How detergent impacts membrane proteins: Atomic-level
views of mitochondrial carriers in dodecylphosphocholine,” The Journal of Physical
Chemistry Letters, vol. 9, no. 5. American Chemical Society, pp. 933–938,
2018.'
ista: 'Kurauskas V, Hessel A, Ma P, Lunetti P, Weinhäupl K, Imbert L, Brutscher
B, King MS, Sounier R, Dolce V, Kunji ERS, Capobianco L, Chipot C, Dehez F, Bersch
B, Schanda P. 2018. How detergent impacts membrane proteins: Atomic-level views
of mitochondrial carriers in dodecylphosphocholine. The Journal of Physical Chemistry
Letters. 9(5), 933–938.'
mla: 'Kurauskas, Vilius, et al. “How Detergent Impacts Membrane Proteins: Atomic-Level
Views of Mitochondrial Carriers in Dodecylphosphocholine.” The Journal of Physical
Chemistry Letters, vol. 9, no. 5, American Chemical Society, 2018, pp. 933–38,
doi:10.1021/acs.jpclett.8b00269.'
short: V. Kurauskas, A. Hessel, P. Ma, P. Lunetti, K. Weinhäupl, L. Imbert, B. Brutscher,
M.S. King, R. Sounier, V. Dolce, E.R.S. Kunji, L. Capobianco, C. Chipot, F. Dehez,
B. Bersch, P. Schanda, The Journal of Physical Chemistry Letters 9 (2018) 933–938.
date_created: 2020-09-18T10:05:45Z
date_published: 2018-02-03T00:00:00Z
date_updated: 2021-01-12T08:19:18Z
day: '03'
doi: 10.1021/acs.jpclett.8b00269
extern: '1'
intvolume: ' 9'
issue: '5'
keyword:
- General Materials Science
language:
- iso: eng
month: '02'
oa_version: None
page: 933-938
publication: The Journal of Physical Chemistry Letters
publication_identifier:
issn:
- 1948-7185
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
status: public
title: 'How detergent impacts membrane proteins: Atomic-level views of mitochondrial
carriers in dodecylphosphocholine'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 9
year: '2018'
...
---
_id: '8440'
abstract:
- lang: eng
text: Mycobacterium tuberculosis can remain dormant in the host, an ability that
explains the failure of many current tuberculosis treatments. Recently, the natural
products cyclomarin, ecumicin, and lassomycin have been shown to efficiently kill
Mycobacterium tuberculosis persisters. Their target is the N-terminal domain of
the hexameric AAA+ ATPase ClpC1, which recognizes, unfolds, and translocates protein
substrates, such as proteins containing phosphorylated arginine residues, to the
ClpP1P2 protease for degradation. Surprisingly, these antibiotics do not inhibit
ClpC1 ATPase activity, and how they cause cell death is still unclear. Here, using
NMR and small-angle X-ray scattering, we demonstrate that arginine-phosphate binding
to the ClpC1 N-terminal domain induces millisecond dynamics. We show that these
dynamics are caused by conformational changes and do not result from unfolding
or oligomerization of this domain. Cyclomarin binding to this domain specifically
blocked these N-terminal dynamics. On the basis of these results, we propose a
mechanism of action involving cyclomarin-induced restriction of ClpC1 dynamics,
which modulates the chaperone enzymatic activity leading eventually to cell death.
article_processing_charge: No
article_type: original
author:
- first_name: Katharina
full_name: Weinhäupl, Katharina
last_name: Weinhäupl
- first_name: Martha
full_name: Brennich, Martha
last_name: Brennich
- first_name: Uli
full_name: Kazmaier, Uli
last_name: Kazmaier
- first_name: Joel
full_name: Lelievre, Joel
last_name: Lelievre
- first_name: Lluis
full_name: Ballell, Lluis
last_name: Ballell
- first_name: Alfred
full_name: Goldberg, Alfred
last_name: Goldberg
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Hugo
full_name: Fraga, Hugo
last_name: Fraga
citation:
ama: Weinhäupl K, Brennich M, Kazmaier U, et al. The antibiotic cyclomarin blocks
arginine-phosphate–induced millisecond dynamics in the N-terminal domain of ClpC1
from Mycobacterium tuberculosis. Journal of Biological Chemistry. 2018;293(22):8379-8393.
doi:10.1074/jbc.ra118.002251
apa: Weinhäupl, K., Brennich, M., Kazmaier, U., Lelievre, J., Ballell, L., Goldberg,
A., … Fraga, H. (2018). The antibiotic cyclomarin blocks arginine-phosphate–induced
millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis.
Journal of Biological Chemistry. American Society for Biochemistry &
Molecular Biology. https://doi.org/10.1074/jbc.ra118.002251
chicago: Weinhäupl, Katharina, Martha Brennich, Uli Kazmaier, Joel Lelievre, Lluis
Ballell, Alfred Goldberg, Paul Schanda, and Hugo Fraga. “The Antibiotic Cyclomarin
Blocks Arginine-Phosphate–Induced Millisecond Dynamics in the N-Terminal Domain
of ClpC1 from Mycobacterium Tuberculosis.” Journal of Biological Chemistry.
American Society for Biochemistry & Molecular Biology, 2018. https://doi.org/10.1074/jbc.ra118.002251.
ieee: K. Weinhäupl et al., “The antibiotic cyclomarin blocks arginine-phosphate–induced
millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis,”
Journal of Biological Chemistry, vol. 293, no. 22. American Society for
Biochemistry & Molecular Biology, pp. 8379–8393, 2018.
ista: Weinhäupl K, Brennich M, Kazmaier U, Lelievre J, Ballell L, Goldberg A, Schanda
P, Fraga H. 2018. The antibiotic cyclomarin blocks arginine-phosphate–induced
millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis.
Journal of Biological Chemistry. 293(22), 8379–8393.
mla: Weinhäupl, Katharina, et al. “The Antibiotic Cyclomarin Blocks Arginine-Phosphate–Induced
Millisecond Dynamics in the N-Terminal Domain of ClpC1 from Mycobacterium Tuberculosis.”
Journal of Biological Chemistry, vol. 293, no. 22, American Society for
Biochemistry & Molecular Biology, 2018, pp. 8379–93, doi:10.1074/jbc.ra118.002251.
short: K. Weinhäupl, M. Brennich, U. Kazmaier, J. Lelievre, L. Ballell, A. Goldberg,
P. Schanda, H. Fraga, Journal of Biological Chemistry 293 (2018) 8379–8393.
date_created: 2020-09-18T10:05:18Z
date_published: 2018-06-01T00:00:00Z
date_updated: 2021-01-12T08:19:17Z
day: '01'
doi: 10.1074/jbc.ra118.002251
extern: '1'
intvolume: ' 293'
issue: '22'
keyword:
- Cell Biology
- Biochemistry
- Molecular Biology
language:
- iso: eng
month: '06'
oa_version: None
page: 8379-8393
publication: Journal of Biological Chemistry
publication_identifier:
issn:
- 0021-9258
- 1083-351X
publication_status: published
publisher: American Society for Biochemistry & Molecular Biology
quality_controlled: '1'
status: public
title: The antibiotic cyclomarin blocks arginine-phosphate–induced millisecond dynamics
in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 293
year: '2018'
...
---
_id: '8442'
abstract:
- lang: eng
text: Membrane proteins perform a host of vital cellular functions. Deciphering
the molecular mechanisms whereby they fulfill these functions requires detailed
biophysical and structural investigations. Detergents have proven pivotal to extract
the protein from its native surroundings. Yet, they provide a milieu that departs
significantly from that of the biological membrane, to the extent that the structure,
the dynamics, and the interactions of membrane proteins in detergents may considerably
vary, as compared to the native environment. Understanding the impact of detergents
on membrane proteins is, therefore, crucial to assess the biological relevance
of results obtained in detergents. Here, we review the strengths and weaknesses
of alkyl phosphocholines (or foscholines), the most widely used detergent in solution-NMR
studies of membrane proteins. While this class of detergents is often successful
for membrane protein solubilization, a growing list of examples points to destabilizing
and denaturing properties, in particular for α-helical membrane proteins. Our
comprehensive analysis stresses the importance of stringent controls when working
with this class of detergents and when analyzing the structure and dynamics of
membrane proteins in alkyl phosphocholine detergents.
article_processing_charge: No
article_type: original
author:
- first_name: Christophe
full_name: Chipot, Christophe
last_name: Chipot
- first_name: François
full_name: Dehez, François
last_name: Dehez
- first_name: Jason R.
full_name: Schnell, Jason R.
last_name: Schnell
- first_name: Nicole
full_name: Zitzmann, Nicole
last_name: Zitzmann
- first_name: Eva
full_name: Pebay-Peyroula, Eva
last_name: Pebay-Peyroula
- first_name: Laurent J.
full_name: Catoire, Laurent J.
last_name: Catoire
- first_name: Bruno
full_name: Miroux, Bruno
last_name: Miroux
- first_name: Edmund R. S.
full_name: Kunji, Edmund R. S.
last_name: Kunji
- first_name: Gianluigi
full_name: Veglia, Gianluigi
last_name: Veglia
- first_name: Timothy A.
full_name: Cross, Timothy A.
last_name: Cross
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: 'Chipot C, Dehez F, Schnell JR, et al. Perturbations of native membrane protein
structure in alkyl phosphocholine detergents: A critical assessment of NMR and
biophysical studies. Chemical Reviews. 2018;118(7):3559-3607. doi:10.1021/acs.chemrev.7b00570'
apa: 'Chipot, C., Dehez, F., Schnell, J. R., Zitzmann, N., Pebay-Peyroula, E., Catoire,
L. J., … Schanda, P. (2018). Perturbations of native membrane protein structure
in alkyl phosphocholine detergents: A critical assessment of NMR and biophysical
studies. Chemical Reviews. American Chemical Society. https://doi.org/10.1021/acs.chemrev.7b00570'
chicago: 'Chipot, Christophe, François Dehez, Jason R. Schnell, Nicole Zitzmann,
Eva Pebay-Peyroula, Laurent J. Catoire, Bruno Miroux, et al. “Perturbations of
Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical
Assessment of NMR and Biophysical Studies.” Chemical Reviews. American
Chemical Society, 2018. https://doi.org/10.1021/acs.chemrev.7b00570.'
ieee: 'C. Chipot et al., “Perturbations of native membrane protein structure
in alkyl phosphocholine detergents: A critical assessment of NMR and biophysical
studies,” Chemical Reviews, vol. 118, no. 7. American Chemical Society,
pp. 3559–3607, 2018.'
ista: 'Chipot C, Dehez F, Schnell JR, Zitzmann N, Pebay-Peyroula E, Catoire LJ,
Miroux B, Kunji ERS, Veglia G, Cross TA, Schanda P. 2018. Perturbations of native
membrane protein structure in alkyl phosphocholine detergents: A critical assessment
of NMR and biophysical studies. Chemical Reviews. 118(7), 3559–3607.'
mla: 'Chipot, Christophe, et al. “Perturbations of Native Membrane Protein Structure
in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical
Studies.” Chemical Reviews, vol. 118, no. 7, American Chemical Society,
2018, pp. 3559–607, doi:10.1021/acs.chemrev.7b00570.'
short: C. Chipot, F. Dehez, J.R. Schnell, N. Zitzmann, E. Pebay-Peyroula, L.J. Catoire,
B. Miroux, E.R.S. Kunji, G. Veglia, T.A. Cross, P. Schanda, Chemical Reviews 118
(2018) 3559–3607.
date_created: 2020-09-18T10:05:35Z
date_published: 2018-02-28T00:00:00Z
date_updated: 2021-01-12T08:19:18Z
day: '28'
doi: 10.1021/acs.chemrev.7b00570
extern: '1'
intvolume: ' 118'
issue: '7'
keyword:
- General Chemistry
language:
- iso: eng
month: '02'
oa_version: None
page: 3559-3607
publication: Chemical Reviews
publication_identifier:
issn:
- 0009-2665
- 1520-6890
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
status: public
title: 'Perturbations of native membrane protein structure in alkyl phosphocholine
detergents: A critical assessment of NMR and biophysical studies'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 118
year: '2018'
...
---
_id: '8441'
abstract:
- lang: eng
text: Solid-state near-rotary-resonance measurements of the spin–lattice relaxation
rate in the rotating frame (R1ρ) is a powerful NMR technique for studying molecular
dynamics in the microsecond time scale. The small difference between the spin-lock
(SL) and magic-angle-spinning (MAS) frequencies allows sampling very slow motions,
at the same time it brings up some methodological challenges. In this work, several
issues affecting correct measurements and analysis of 15N R1ρ data are considered
in detail. Among them are signal amplitude as a function of the difference between
SL and MAS frequencies, “dead time” in the initial part of the relaxation decay
caused by transient spin-dynamic oscillations, measurements under HORROR condition
and proper treatment of the multi-exponential relaxation decays. The multiple
15N R1ρ measurements at different SL fields and temperatures have been conducted
in 1D mode (i.e. without site-specific resolution) for a set of four different
microcrystalline protein samples (GB1, SH3, MPD-ubiquitin and cubic-PEG-ubiquitin)
to study the overall protein rocking in a crystal. While the amplitude of this
motion varies very significantly, its correlation time for all four sample is
practically the same, 30–50 μs. The amplitude of the rocking motion correlates
with the packing density of a protein crystal. It has been suggested that the
rocking motion is not diffusive but likely a jump-like dynamic process.
article_processing_charge: No
article_type: original
author:
- first_name: Alexey
full_name: Krushelnitsky, Alexey
last_name: Krushelnitsky
- first_name: Diego
full_name: Gauto, Diego
last_name: Gauto
- first_name: Diana C.
full_name: Rodriguez Camargo, Diana C.
last_name: Rodriguez Camargo
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Kay
full_name: Saalwächter, Kay
last_name: Saalwächter
citation:
ama: 'Krushelnitsky A, Gauto D, Rodriguez Camargo DC, Schanda P, Saalwächter K.
Microsecond motions probed by near-rotary-resonance R1ρ 15N MAS NMR experiments:
The model case of protein overall-rocking in crystals. Journal of Biomolecular
NMR. 2018;71(1):53-67. doi:10.1007/s10858-018-0191-4'
apa: 'Krushelnitsky, A., Gauto, D., Rodriguez Camargo, D. C., Schanda, P., &
Saalwächter, K. (2018). Microsecond motions probed by near-rotary-resonance R1ρ
15N MAS NMR experiments: The model case of protein overall-rocking in crystals.
Journal of Biomolecular NMR. Springer Nature. https://doi.org/10.1007/s10858-018-0191-4'
chicago: 'Krushelnitsky, Alexey, Diego Gauto, Diana C. Rodriguez Camargo, Paul Schanda,
and Kay Saalwächter. “Microsecond Motions Probed by Near-Rotary-Resonance R1ρ
15N MAS NMR Experiments: The Model Case of Protein Overall-Rocking in Crystals.”
Journal of Biomolecular NMR. Springer Nature, 2018. https://doi.org/10.1007/s10858-018-0191-4.'
ieee: 'A. Krushelnitsky, D. Gauto, D. C. Rodriguez Camargo, P. Schanda, and K. Saalwächter,
“Microsecond motions probed by near-rotary-resonance R1ρ 15N MAS NMR experiments:
The model case of protein overall-rocking in crystals,” Journal of Biomolecular
NMR, vol. 71, no. 1. Springer Nature, pp. 53–67, 2018.'
ista: 'Krushelnitsky A, Gauto D, Rodriguez Camargo DC, Schanda P, Saalwächter K.
2018. Microsecond motions probed by near-rotary-resonance R1ρ 15N MAS NMR experiments:
The model case of protein overall-rocking in crystals. Journal of Biomolecular
NMR. 71(1), 53–67.'
mla: 'Krushelnitsky, Alexey, et al. “Microsecond Motions Probed by Near-Rotary-Resonance
R1ρ 15N MAS NMR Experiments: The Model Case of Protein Overall-Rocking in Crystals.”
Journal of Biomolecular NMR, vol. 71, no. 1, Springer Nature, 2018, pp.
53–67, doi:10.1007/s10858-018-0191-4.'
short: A. Krushelnitsky, D. Gauto, D.C. Rodriguez Camargo, P. Schanda, K. Saalwächter,
Journal of Biomolecular NMR 71 (2018) 53–67.
date_created: 2020-09-18T10:05:28Z
date_published: 2018-05-30T00:00:00Z
date_updated: 2021-01-12T08:19:17Z
day: '30'
doi: 10.1007/s10858-018-0191-4
extern: '1'
intvolume: ' 71'
issue: '1'
language:
- iso: eng
month: '05'
oa_version: Published Version
page: 53-67
publication: Journal of Biomolecular NMR
publication_identifier:
issn:
- 0925-2738
- 1573-5001
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: 'Microsecond motions probed by near-rotary-resonance R1ρ 15N MAS NMR experiments:
The model case of protein overall-rocking in crystals'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 71
year: '2018'
...
---
_id: '8439'
abstract:
- lang: eng
text: Lipopolysaccharides (LPS) are complex glycolipids forming the outside layer
of Gram-negative bacteria. Their hydrophobic and heterogeneous nature greatly
hampers their structural study in an environment similar to the bacterial surface.
We have studied LPS purified from E. coli and pathogenic P. aeruginosa with long
O-antigen polysaccharides assembled in solution as vesicles or elongated micelles.
Solid-state NMR with magic-angle spinning permitted the identification of NMR
signals arising from regions with different flexibilities in the LPS, from the
lipid components to the O-antigen polysaccharides. Atomic scale data on the LPS
enabled the study of the interaction of gentamicin antibiotic bound to P. aeruginosa
LPS, for which we could confirm that a specific oligosaccharide is involved in
the antibiotic binding. The possibility to study LPS alone and bound to a ligand
when it is assembled in membrane-like structures opens great prospects for the
investigation of proteins and antibiotics that specifically target such an important
molecule at the surface of Gram-negative bacteria.
article_processing_charge: No
article_type: original
author:
- first_name: Cedric
full_name: Laguri, Cedric
last_name: Laguri
- first_name: Alba
full_name: Silipo, Alba
last_name: Silipo
- first_name: Alessandra M.
full_name: Martorana, Alessandra M.
last_name: Martorana
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Roberta
full_name: Marchetti, Roberta
last_name: Marchetti
- first_name: Alessandra
full_name: Polissi, Alessandra
last_name: Polissi
- first_name: Antonio
full_name: Molinaro, Antonio
last_name: Molinaro
- first_name: Jean-Pierre
full_name: Simorre, Jean-Pierre
last_name: Simorre
citation:
ama: Laguri C, Silipo A, Martorana AM, et al. Solid state NMR studies of intact
lipopolysaccharide endotoxin. ACS Chemical Biology. 2018;13(8):2106-2113.
doi:10.1021/acschembio.8b00271
apa: Laguri, C., Silipo, A., Martorana, A. M., Schanda, P., Marchetti, R., Polissi,
A., … Simorre, J.-P. (2018). Solid state NMR studies of intact lipopolysaccharide
endotoxin. ACS Chemical Biology. American Chemical Society. https://doi.org/10.1021/acschembio.8b00271
chicago: Laguri, Cedric, Alba Silipo, Alessandra M. Martorana, Paul Schanda, Roberta
Marchetti, Alessandra Polissi, Antonio Molinaro, and Jean-Pierre Simorre. “Solid
State NMR Studies of Intact Lipopolysaccharide Endotoxin.” ACS Chemical Biology.
American Chemical Society, 2018. https://doi.org/10.1021/acschembio.8b00271.
ieee: C. Laguri et al., “Solid state NMR studies of intact lipopolysaccharide
endotoxin,” ACS Chemical Biology, vol. 13, no. 8. American Chemical Society,
pp. 2106–2113, 2018.
ista: Laguri C, Silipo A, Martorana AM, Schanda P, Marchetti R, Polissi A, Molinaro
A, Simorre J-P. 2018. Solid state NMR studies of intact lipopolysaccharide endotoxin.
ACS Chemical Biology. 13(8), 2106–2113.
mla: Laguri, Cedric, et al. “Solid State NMR Studies of Intact Lipopolysaccharide
Endotoxin.” ACS Chemical Biology, vol. 13, no. 8, American Chemical Society,
2018, pp. 2106–13, doi:10.1021/acschembio.8b00271.
short: C. Laguri, A. Silipo, A.M. Martorana, P. Schanda, R. Marchetti, A. Polissi,
A. Molinaro, J.-P. Simorre, ACS Chemical Biology 13 (2018) 2106–2113.
date_created: 2020-09-18T10:05:09Z
date_published: 2018-07-02T00:00:00Z
date_updated: 2021-01-12T08:19:16Z
day: '02'
doi: 10.1021/acschembio.8b00271
extern: '1'
intvolume: ' 13'
issue: '8'
keyword:
- Molecular Medicine
- Biochemistry
- General Medicine
language:
- iso: eng
month: '07'
oa_version: None
page: 2106-2113
publication: ACS Chemical Biology
publication_identifier:
issn:
- 1554-8929
- 1554-8937
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
status: public
title: Solid state NMR studies of intact lipopolysaccharide endotoxin
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 13
year: '2018'
...