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Arginine Side-Chain Hydrogen Exchange: Quantifying Arginine Side-Chain Interactions in Solution

Mackenzie, HW; Flemming Hansen, D; (2019) Arginine Side-Chain Hydrogen Exchange: Quantifying Arginine Side-Chain Interactions in Solution. ChemPhysChem , 20 (2) , Article Special Issue: BioNMR Spectroscopy. 10.1002/cphc.201800598. Green open access

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Abstract

The rate with which labile backbone hydrogen atoms in proteins exchange with the solvent has long been used to probe protein interactions in aqueous solutions. Arginine, an essential amino acid found in many interaction interfaces, is capable of an impressive range of interactions via its guanidinium group. The hydrogen exchange rate of the guanidinium hydrogens therefore becomes an important measure to quantify side-chain interactions. Herein we present an NMR method to quantify the hydrogen exchange rates of arginine side-chain 1 Hϵ protons and thus present a method to gauge the strength of arginine side-chain interactions. The method employs 13 C-detection and the one-bond deuterium isotope shift observed for 15 Nϵ to generate two exchanging species in 1 H2 O/2 H2 O mixtures. An application to the protein T4 Lysozyme is shown, where protection factors calculated from the obtained exchange rates correlate well with the interactions observed in the crystal structure. The methodology presented provides an important step towards characterising interactions of arginine side-chains in enzymes, in phase separation, and in protein interaction interfaces in general.

Type: Article
Title: Arginine Side-Chain Hydrogen Exchange: Quantifying Arginine Side-Chain Interactions in Solution
Open access status: An open access version is available from UCL Discovery
DOI: 10.1002/cphc.201800598
Publisher version: https://doi.org/10.1002/cphc.201800598
Language: English
Additional information: This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/ licenses/ by/4.0/.
Keywords: 13C-detected NMR spectroscopy, arginine side-chains, guanidinium interactions, hydrogen exchange, protection factors, protein-protein interactions
UCL classification: UCL
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences > Structural and Molecular Biology
URI: https://discovery.ucl.ac.uk/id/eprint/10058654
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