A high-field cellular DNP-supported solid-state NMR approach to
study proteins with sub-cellular specificity

J 2023

A high-field cellular DNP-supported solid-state NMR approach to study proteins with sub-cellular specificity

BERIASHVILI, David; Ru YAO; Francesca D'AMICO; Michaela DZUROV KRAFČÍKOVÁ; Andrei GURINOV et al.

Základní údaje

Originální název

A high-field cellular DNP-supported solid-state NMR approach to study proteins with sub-cellular specificity

Autoři

BERIASHVILI, David; Ru YAO; Francesca D'AMICO; Michaela DZUROV KRAFČÍKOVÁ ; Andrei GURINOV; Adil SAFEER; Xinyi CAI; Monique P. C. MULDER; Yangping LIU; Gert E. FOLKERS a Marc BALDUS

Vydání

CHEMICAL SCIENCE, CAMBRIDGE, ROYAL SOC CHEMISTRY, 2023, 2041-6520

Další údaje

Typ výsledku

Článek v odborném periodiku

Impakt faktor

Impact factor: 7.600

Označené pro přenos do RIV

DOI

https://doi.org/10.1039/d3sc02117c

UT WoS

001058349500001

Změněno: 20. 1. 2026 15:11, Mgr. Michaela Dzurov Krafčíková, Ph.D.

Anotace

V originále

Studying the structural aspects of proteins within sub-cellular compartments is of growing interest. Dynamic nuclear polarization supported solid-state NMR (DNP-ssNMR) is uniquely suited to provide such information, but critically lacks the desired sensitivity and resolution. Here we utilize SNAPol-1, a novel biradical, to conduct DNP-ssNMR at high-magnetic fields (800 MHz/527 GHz) inside HeLa cells and isolated cell nuclei electroporated with [13C,15N] labeled ubiquitin. We report that SNAPol-1 passively diffuses and homogenously distributes within whole cells and cell nuclei providing ubiquitin spectra of high sensitivity and remarkably improved spectral resolution. For cell nuclei, physical enrichment facilitates a further 4-fold decrease in measurement time and provides an exclusive structural view of the nuclear ubiquitin pool. Taken together, these advancements enable atomic interrogation of protein conformational plasticity at atomic resolution and with sub-cellular specificity.

Citovat

BERIASHVILI, David; Ru YAO; Francesca D'AMICO; Michaela DZUROV KRAFČÍKOVÁ; Andrei GURINOV; Adil SAFEER; Xinyi CAI; Monique P. C. MULDER; Yangping LIU; Gert E. FOLKERS a Marc BALDUS. A high-field cellular DNP-supported solid-state NMR approach to study proteins with sub-cellular specificity. CHEMICAL SCIENCE. CAMBRIDGE: ROYAL SOC CHEMISTRY, 2023, roč. 14, č. 36, s. 9892-9899. ISSN 2041-6520. Dostupné z: https://doi.org/10.1039/d3sc02117c.

@article{2526338,
   author = {Beriashvili, David and Yao, Ru and D'Amico, Francesca and Dzurov Krafčíková, Michaela and Gurinov, Andrei and Safeer, Adil and Cai, Xinyi and Mulder, Monique P. C. and Liu, Yangping and Folkers, Gert E. and Baldus, Marc},
   article_location = {CAMBRIDGE},
   article_number = {36},
   doi = {https://doi.org/10.1039/d3sc02117c},
   issn = {2041-6520},
   journal = {CHEMICAL SCIENCE},
   title = {A high-field cellular DNP-supported solid-state NMR approach to study proteins with sub-cellular specificity},
   volume = {14},
   year = {2023}
}

TY  - JOUR
ID  - 2526338
AU  - Beriashvili, David - Yao, Ru - D'Amico, Francesca - Dzurov Krafčíková, Michaela - Gurinov, Andrei - Safeer, Adil - Cai, Xinyi - Mulder, Monique P. C. - Liu, Yangping - Folkers, Gert E. - Baldus, Marc
PY  - 2023
TI  - A high-field cellular DNP-supported solid-state NMR approach to study proteins with sub-cellular specificity
JF  - CHEMICAL SCIENCE
VL  - 14
IS  - 36
SP  - 9892-9899
EP  - 9892-9899
PB  - ROYAL SOC CHEMISTRY
SN  - 20416520
N2  - Studying the structural aspects of proteins within sub-cellular compartments is of growing interest. Dynamic nuclear polarization supported solid-state NMR (DNP-ssNMR) is uniquely suited to provide such information, but critically lacks the desired sensitivity and resolution. Here we utilize SNAPol-1, a novel biradical, to conduct DNP-ssNMR at high-magnetic fields (800 MHz/527 GHz) inside HeLa cells and isolated cell nuclei electroporated with [13C,15N] labeled ubiquitin. We report that SNAPol-1 passively diffuses and homogenously distributes within whole cells and cell nuclei providing ubiquitin spectra of high sensitivity and remarkably improved spectral resolution. For cell nuclei, physical enrichment facilitates a further 4-fold decrease in measurement time and provides an exclusive structural view of the nuclear ubiquitin pool. Taken together, these advancements enable atomic interrogation of protein conformational plasticity at atomic resolution and with sub-cellular specificity.
ER  -

BERIASHVILI, David; Ru YAO; Francesca D'AMICO; Michaela DZUROV KRAFČÍKOVÁ; Andrei GURINOV; Adil SAFEER; Xinyi CAI; Monique P. C. MULDER; Yangping LIU; Gert E. FOLKERS a Marc BALDUS. A high-field cellular DNP-supported solid-state NMR approach to study proteins with sub-cellular specificity. \textit{CHEMICAL SCIENCE}. CAMBRIDGE: ROYAL SOC CHEMISTRY, 2023, roč.~14, č.~36, s.~9892-9899. ISSN~2041-6520. Dostupné z: https://doi.org/10.1039/d3sc02117c.

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