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Organoarsenic probes to study proteins by NMR spectroscopy

29 November 2021, Version 1
Working Paper
This content is a preprint and has not undergone peer review at the time of posting.

Abstract

Arsenical probes enable structural studies of proteins. We report the first organoarsenic probes for nuclear magnetic resonance (NMR) 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.

Supplementary materials

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Supporting Information
Description
Detailed procedures and conditions for probe synthesis, protein expression and purification, sample preparation; tables of PCSs and fitted tensor parameters; correlations between back-calculated and measured PCSs; mass spectrometry data; EPR data.
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Now Published

Organoarsenic probes to study proteins by NMR spectroscopy [opens in a new tab]
Mithun C. Mahawaththa, Henry W. Orton, Ibidolapo Adekoya, Thomas Huber, Gottfried Otting, Christoph Nitsche journal article
Chemical Communications , Volume 58, Issue 5
Online publication date: 2022

Version History

Nov 29, 2021 Version 1

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The content is available under CC BY NC ND 4.0 [opens in a new tab]

DOI

10.26434/chemrxiv-2021-48dn4
D O I: 10.26434/chemrxiv-2021-48dn4 [opens in a new tab]

Funding

Australian Research Council
DE190100015; DP200100348; FL170100019; CE200100012
Alexander von Humboldt-Stiftung
Feodor Lynen Research Fellowship

Author’s competing interest statement

The author(s) have declared they have no conflict of interest with regard to this content

Ethics

The author(s) have declared ethics committee/IRB approval is not relevant to this content

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