NMR Spectroscopic Assignment of Backbone and Side-Chain Protons in Fully Protonated Proteins: Microcrystals, Sedimented Assemblies, and Amyloid Fibrils

Jan Stanek; Loren B. Andreas; Kristaps Jaudzems; Diane Cala; Daniela Lalli; Andrea Bertarello; Tobias Schubeis; Inara Akopjana; Svetlana Kotelovica; Kaspars Tars; Andrea Pica; Serena Leone; Delia Picone; Zhi Qiang Xu; Nicholas E. Dixon; Denis Martinez; Mélanie Berbon; Nadia El Mammeri; Abdelmajid Noubhani; Sven Saupe; Birgit Habenstein; Antoine Loquet; Guido Pintacuda

doi:10.1002/anie.201607084

NMR Spectroscopic Assignment of Backbone and Side-Chain Protons in Fully Protonated Proteins: Microcrystals, Sedimented Assemblies, and Amyloid Fibrils

Jan Stanek, Loren B. Andreas, Kristaps Jaudzems, Diane Cala, Daniela Lalli, Andrea Bertarello, Tobias Schubeis, Inara Akopjana, Svetlana Kotelovica, Kaspars Tars, Andrea Pica, Serena Leone, Delia Picone, Zhi Qiang Xu, Nicholas E. Dixon, Denis Martinez, Mélanie Berbon, Nadia El Mammeri, Abdelmajid Noubhani, Sven SaupeBirgit Habenstein, Antoine Loquet, Guido Pintacuda

Risultato della ricerca: Contributo su rivista › Articolo in rivista › peer review

Abstract

We demonstrate sensitive detection of alpha protons of fully protonated proteins by solid-state NMR spectroscopy with 100–111 kHz magic-angle spinning (MAS). The excellent resolution in the Cα-Hα plane is demonstrated for 5 proteins, including microcrystals, a sedimented complex, a capsid and amyloid fibrils. A set of 3D spectra based on a Cα–Hα detection block was developed and applied for the sequence-specific backbone and aliphatic side-chain resonance assignment using only 500 μg of sample. These developments accelerate structural studies of biomolecular assemblies available in submilligram quantities without the need of protein deuteration.

Lingua originale	Inglese
pagine (da-a)	15504-15509
Numero di pagine	6
Rivista	Angewandte Chemie - International Edition
Volume	55
Numero di pubblicazione	50
DOI	https://doi.org/10.1002/anie.201607084
Stato di pubblicazione	Pubblicato - 12 dic 2016
Pubblicato esternamente	Sì

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10.1002/anie.201607084

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Stanek, J., Andreas, L. B., Jaudzems, K., Cala, D., Lalli, D., Bertarello, A., Schubeis, T., Akopjana, I., Kotelovica, S., Tars, K., Pica, A., Leone, S., Picone, D., Xu, Z. Q., Dixon, N. E., Martinez, D., Berbon, M., El Mammeri, N., Noubhani, A., ... Pintacuda, G. (2016). NMR Spectroscopic Assignment of Backbone and Side-Chain Protons in Fully Protonated Proteins: Microcrystals, Sedimented Assemblies, and Amyloid Fibrils. Angewandte Chemie - International Edition, 55(50), 15504-15509. https://doi.org/10.1002/anie.201607084

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title = "NMR Spectroscopic Assignment of Backbone and Side-Chain Protons in Fully Protonated Proteins: Microcrystals, Sedimented Assemblies, and Amyloid Fibrils",

abstract = "We demonstrate sensitive detection of alpha protons of fully protonated proteins by solid-state NMR spectroscopy with 100–111 kHz magic-angle spinning (MAS). The excellent resolution in the Cα-Hα plane is demonstrated for 5 proteins, including microcrystals, a sedimented complex, a capsid and amyloid fibrils. A set of 3D spectra based on a Cα–Hα detection block was developed and applied for the sequence-specific backbone and aliphatic side-chain resonance assignment using only 500 μg of sample. These developments accelerate structural studies of biomolecular assemblies available in submilligram quantities without the need of protein deuteration.",

keywords = "magic-angle spinning, proton detection, resonance assignment, solid-state NMR spectroscopy",

author = "Jan Stanek and Andreas, {Loren B.} and Kristaps Jaudzems and Diane Cala and Daniela Lalli and Andrea Bertarello and Tobias Schubeis and Inara Akopjana and Svetlana Kotelovica and Kaspars Tars and Andrea Pica and Serena Leone and Delia Picone and Xu, {Zhi Qiang} and Dixon, {Nicholas E.} and Denis Martinez and M{\'e}lanie Berbon and {El Mammeri}, Nadia and Abdelmajid Noubhani and Sven Saupe and Birgit Habenstein and Antoine Loquet and Guido Pintacuda",

note = "Publisher Copyright: {\textcopyright} 2016 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim",

year = "2016",

month = dec,

day = "12",

doi = "10.1002/anie.201607084",

language = "English",

volume = "55",

pages = "15504--15509",

journal = "Angewandte Chemie - International Edition",

issn = "1433-7851",

publisher = "John Wiley and Sons Ltd",

number = "50",

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Stanek, J, Andreas, LB, Jaudzems, K, Cala, D, Lalli, D, Bertarello, A, Schubeis, T, Akopjana, I, Kotelovica, S, Tars, K, Pica, A, Leone, S, Picone, D, Xu, ZQ, Dixon, NE, Martinez, D, Berbon, M, El Mammeri, N, Noubhani, A, Saupe, S, Habenstein, B, Loquet, A & Pintacuda, G 2016, 'NMR Spectroscopic Assignment of Backbone and Side-Chain Protons in Fully Protonated Proteins: Microcrystals, Sedimented Assemblies, and Amyloid Fibrils', Angewandte Chemie - International Edition, vol. 55, n. 50, pagg. 15504-15509. https://doi.org/10.1002/anie.201607084

NMR Spectroscopic Assignment of Backbone and Side-Chain Protons in Fully Protonated Proteins: Microcrystals, Sedimented Assemblies, and Amyloid Fibrils. / Stanek, Jan; Andreas, Loren B.; Jaudzems, Kristaps et al.
In: Angewandte Chemie - International Edition, Vol. 55, N. 50, 12.12.2016, pag. 15504-15509.

Risultato della ricerca: Contributo su rivista › Articolo in rivista › peer review

TY - JOUR

T1 - NMR Spectroscopic Assignment of Backbone and Side-Chain Protons in Fully Protonated Proteins

T2 - Microcrystals, Sedimented Assemblies, and Amyloid Fibrils

AU - Stanek, Jan

AU - Andreas, Loren B.

AU - Jaudzems, Kristaps

AU - Cala, Diane

AU - Lalli, Daniela

AU - Bertarello, Andrea

AU - Schubeis, Tobias

AU - Akopjana, Inara

AU - Kotelovica, Svetlana

AU - Tars, Kaspars

AU - Pica, Andrea

AU - Leone, Serena

AU - Picone, Delia

AU - Xu, Zhi Qiang

AU - Dixon, Nicholas E.

AU - Martinez, Denis

AU - Berbon, Mélanie

AU - El Mammeri, Nadia

AU - Noubhani, Abdelmajid

AU - Saupe, Sven

AU - Habenstein, Birgit

AU - Loquet, Antoine

AU - Pintacuda, Guido

PY - 2016/12/12

Y1 - 2016/12/12

N2 - We demonstrate sensitive detection of alpha protons of fully protonated proteins by solid-state NMR spectroscopy with 100–111 kHz magic-angle spinning (MAS). The excellent resolution in the Cα-Hα plane is demonstrated for 5 proteins, including microcrystals, a sedimented complex, a capsid and amyloid fibrils. A set of 3D spectra based on a Cα–Hα detection block was developed and applied for the sequence-specific backbone and aliphatic side-chain resonance assignment using only 500 μg of sample. These developments accelerate structural studies of biomolecular assemblies available in submilligram quantities without the need of protein deuteration.

AB - We demonstrate sensitive detection of alpha protons of fully protonated proteins by solid-state NMR spectroscopy with 100–111 kHz magic-angle spinning (MAS). The excellent resolution in the Cα-Hα plane is demonstrated for 5 proteins, including microcrystals, a sedimented complex, a capsid and amyloid fibrils. A set of 3D spectra based on a Cα–Hα detection block was developed and applied for the sequence-specific backbone and aliphatic side-chain resonance assignment using only 500 μg of sample. These developments accelerate structural studies of biomolecular assemblies available in submilligram quantities without the need of protein deuteration.

KW - magic-angle spinning

KW - proton detection

KW - resonance assignment

KW - solid-state NMR spectroscopy

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U2 - 10.1002/anie.201607084

DO - 10.1002/anie.201607084

M3 - Article

SN - 1433-7851

VL - 55

SP - 15504

EP - 15509

JO - Angewandte Chemie - International Edition

JF - Angewandte Chemie - International Edition

IS - 50

ER -

NMR Spectroscopic Assignment of Backbone and Side-Chain Protons in Fully Protonated Proteins: Microcrystals, Sedimented Assemblies, and Amyloid Fibrils

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