HDX-MS: An Analytical Tool to Capture Protein Motion in Action

Virtually all protein functions in the cell, including pathogenic processes, require coordinated motion of atoms or domains, i.e., conformational dynamics. Understanding protein dynamics is therefore critical both for drug development and to learn about the underlying molecular causes of many diseas...

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Main Authors: Dominic Narang, Cristina Lento, Derek J. Wilson
Format: Article
Language:English
Published: MDPI AG 2020-07-01
Series:Biomedicines
Subjects:
Online Access:https://www.mdpi.com/2227-9059/8/7/224
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author Dominic Narang
Cristina Lento
Derek J. Wilson
author_facet Dominic Narang
Cristina Lento
Derek J. Wilson
author_sort Dominic Narang
collection DOAJ
description Virtually all protein functions in the cell, including pathogenic processes, require coordinated motion of atoms or domains, i.e., conformational dynamics. Understanding protein dynamics is therefore critical both for drug development and to learn about the underlying molecular causes of many diseases. Hydrogen–Deuterium Exchange Mass Spectrometry (HDX-MS) provides valuable information about protein dynamics, which is highly complementary to the static picture provided by conventional high-resolution structural tools (i.e., X-ray crystallography and structural NMR). The amount of protein required to carry out HDX-MS experiments is a fraction of the amount required by alternative biophysical techniques, which are also usually lower resolution. Use of HDX-MS is growing quickly both in industry and academia, and it has been successfully used in numerous drug and vaccine development efforts, with important roles in understanding allosteric effects and mapping binding sites.
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spelling doaj.art-e71d04450baf4781ad7f66c70915b97e2023-11-20T07:07:08ZengMDPI AGBiomedicines2227-90592020-07-018722410.3390/biomedicines8070224HDX-MS: An Analytical Tool to Capture Protein Motion in ActionDominic Narang0Cristina Lento1Derek J. Wilson2Department of Chemistry, York University, Toronto, ON M3J 1P3, CanadaDepartment of Chemistry, York University, Toronto, ON M3J 1P3, CanadaDepartment of Chemistry, York University, Toronto, ON M3J 1P3, CanadaVirtually all protein functions in the cell, including pathogenic processes, require coordinated motion of atoms or domains, i.e., conformational dynamics. Understanding protein dynamics is therefore critical both for drug development and to learn about the underlying molecular causes of many diseases. Hydrogen–Deuterium Exchange Mass Spectrometry (HDX-MS) provides valuable information about protein dynamics, which is highly complementary to the static picture provided by conventional high-resolution structural tools (i.e., X-ray crystallography and structural NMR). The amount of protein required to carry out HDX-MS experiments is a fraction of the amount required by alternative biophysical techniques, which are also usually lower resolution. Use of HDX-MS is growing quickly both in industry and academia, and it has been successfully used in numerous drug and vaccine development efforts, with important roles in understanding allosteric effects and mapping binding sites.https://www.mdpi.com/2227-9059/8/7/224hydrogen–deuterium exchange mass spectrometryHDX-MSprotein dynamicsprotein folding and misfolding
spellingShingle Dominic Narang
Cristina Lento
Derek J. Wilson
HDX-MS: An Analytical Tool to Capture Protein Motion in Action
Biomedicines
hydrogen–deuterium exchange mass spectrometry
HDX-MS
protein dynamics
protein folding and misfolding
title HDX-MS: An Analytical Tool to Capture Protein Motion in Action
title_full HDX-MS: An Analytical Tool to Capture Protein Motion in Action
title_fullStr HDX-MS: An Analytical Tool to Capture Protein Motion in Action
title_full_unstemmed HDX-MS: An Analytical Tool to Capture Protein Motion in Action
title_short HDX-MS: An Analytical Tool to Capture Protein Motion in Action
title_sort hdx ms an analytical tool to capture protein motion in action
topic hydrogen–deuterium exchange mass spectrometry
HDX-MS
protein dynamics
protein folding and misfolding
url https://www.mdpi.com/2227-9059/8/7/224
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