Organoarsenic probes to study proteins by NMR spectroscopy

Mithun C. Mahawaththa; Henry W. Orton; Ibidolapo Adekoya; Thomas Huber; Gottfried Otting; Christoph Nitsche

doi:10.1039/d1cc06497e

Organoarsenic probes to study proteins by NMR spectroscopy

Mithun C. Mahawaththa, Henry W. Orton, Ibidolapo Adekoya, Thomas Huber, Gottfried Otting^*, Christoph Nitsche^*

^*Corresponding author for this work

Research School of Chemistry

Research output: Contribution to journal › Article › peer-review

2 Citations (Scopus)

Abstract

Arsenical probes enable structural studies of proteins. We report the first organoarsenic probes for nuclear magnetic resonance (NMR) and electron paramagnetic resonance (EPR) spectroscopy to study proteins in solutions. These probes can be attached to irregular loop regions. A lanthanide-binding tag induces sizable pseudocontact shifts in protein NMR spectra of a magnitude never observed for small paramagnetic probes before.

Original language	English
Pages (from-to)	701-704
Number of pages	4
Journal	Chemical Communications
Volume	58
Issue number	5
DOIs	https://doi.org/10.1039/d1cc06497e
Publication status	Published - 16 Jan 2022

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abstract = "Arsenical probes enable structural studies of proteins. We report the first organoarsenic probes for nuclear magnetic resonance (NMR) and electron paramagnetic resonance (EPR) spectroscopy to study proteins in solutions. These probes can be attached to irregular loop regions. A lanthanide-binding tag induces sizable pseudocontact shifts in protein NMR spectra of a magnitude never observed for small paramagnetic probes before.",

author = "Mahawaththa, {Mithun C.} and Orton, {Henry W.} and Ibidolapo Adekoya and Thomas Huber and Gottfried Otting and Christoph Nitsche",

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AU - Mahawaththa, Mithun C.

AU - Orton, Henry W.

AU - Adekoya, Ibidolapo

AU - Huber, Thomas

AU - Otting, Gottfried

AU - Nitsche, Christoph

PY - 2022/1/16

Y1 - 2022/1/16

N2 - Arsenical probes enable structural studies of proteins. We report the first organoarsenic probes for nuclear magnetic resonance (NMR) and electron paramagnetic resonance (EPR) spectroscopy to study proteins in solutions. These probes can be attached to irregular loop regions. A lanthanide-binding tag induces sizable pseudocontact shifts in protein NMR spectra of a magnitude never observed for small paramagnetic probes before.

AB - Arsenical probes enable structural studies of proteins. We report the first organoarsenic probes for nuclear magnetic resonance (NMR) and electron paramagnetic resonance (EPR) spectroscopy to study proteins in solutions. These probes can be attached to irregular loop regions. A lanthanide-binding tag induces sizable pseudocontact shifts in protein NMR spectra of a magnitude never observed for small paramagnetic probes before.

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SP - 701

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JO - Chemical Communications

JF - Chemical Communications

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Organoarsenic probes to study proteins by NMR spectroscopy

Abstract

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