DNP‐Supported Solid‐State NMR Spectroscopy of Proteins Inside Mammalian Cells

Siddarth Narasimhan; Stephan Scherpe; Alessandra Lucini Paioni; Johan van der Zwan; Gert E. Folkers; Huib Ovaa; Marc Baldus

doi:10.1002/ange.201903246

DNP‐Supported Solid‐State NMR Spectroscopy of Proteins Inside Mammalian Cells

Siddarth Narasimhan, Stephan Scherpe, Alessandra Lucini Paioni, Johan van der Zwan, Gert E. Folkers, Huib Ovaa, Marc Baldus

Research output: Contribution to journal › Article › Academic

Abstract

Elucidating at atomic level how proteins interact and are chemically modified in cells represents a leading frontier in structural biology. We have developed a tailored solid-state NMR spectroscopic approach that allows studying protein structure inside human cells at atomic level under high-sensitivity dynamic nuclear polarization (DNP) conditions. We demonstrate the method using ubiquitin (Ub), which is critically involved in cellular functioning. Our results pave the way for structural studies of larger proteins or protein complexes inside human cells, which have remained elusive to in-cell solution-state NMR spectroscopy due to molecular size limitations.

Original language	English
Pages (from-to)	13103-13107
Number of pages	5
Journal	Angewandte Chemie
Volume	131
Issue number	37
DOIs	https://doi.org/10.1002/ange.201903246
Publication status	Published - 9 Sept 2019

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abstract = "Elucidating at atomic level how proteins interact and are chemically modified in cells represents a leading frontier in structural biology. We have developed a tailored solid-state NMR spectroscopic approach that allows studying protein structure inside human cells at atomic level under high-sensitivity dynamic nuclear polarization (DNP) conditions. We demonstrate the method using ubiquitin (Ub), which is critically involved in cellular functioning. Our results pave the way for structural studies of larger proteins or protein complexes inside human cells, which have remained elusive to in-cell solution-state NMR spectroscopy due to molecular size limitations.",

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AU - Narasimhan, Siddarth

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AU - van der Zwan, Johan

AU - Folkers, Gert E.

AU - Ovaa, Huib

AU - Baldus, Marc

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AB - Elucidating at atomic level how proteins interact and are chemically modified in cells represents a leading frontier in structural biology. We have developed a tailored solid-state NMR spectroscopic approach that allows studying protein structure inside human cells at atomic level under high-sensitivity dynamic nuclear polarization (DNP) conditions. We demonstrate the method using ubiquitin (Ub), which is critically involved in cellular functioning. Our results pave the way for structural studies of larger proteins or protein complexes inside human cells, which have remained elusive to in-cell solution-state NMR spectroscopy due to molecular size limitations.

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ER -

DNP‐Supported Solid‐State NMR Spectroscopy of Proteins Inside Mammalian Cells

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