Cargando…

Investigating the Structural Compaction of Biomolecules Upon Transition to the Gas-Phase Using ESI-TWIMS-MS

Collision cross-section (CCS) measurements obtained from ion mobility spectrometry-mass spectrometry (IMS-MS) analyses often provide useful information concerning a protein’s size and shape and can be complemented by modeling procedures. However, there have been some concerns about the extent to whi...

Descripción completa

Detalles Bibliográficos
Autores principales: Devine, Paul W. A., Fisher, Henry C., Calabrese, Antonio N., Whelan, Fiona, Higazi, Daniel R., Potts, Jennifer R., Lowe, David C., Radford, Sheena E., Ashcroft, Alison E.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer US 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5556138/
https://www.ncbi.nlm.nih.gov/pubmed/28484973
http://dx.doi.org/10.1007/s13361-017-1689-9
_version_ 1783257014099509248
author Devine, Paul W. A.
Fisher, Henry C.
Calabrese, Antonio N.
Whelan, Fiona
Higazi, Daniel R.
Potts, Jennifer R.
Lowe, David C.
Radford, Sheena E.
Ashcroft, Alison E.
author_facet Devine, Paul W. A.
Fisher, Henry C.
Calabrese, Antonio N.
Whelan, Fiona
Higazi, Daniel R.
Potts, Jennifer R.
Lowe, David C.
Radford, Sheena E.
Ashcroft, Alison E.
author_sort Devine, Paul W. A.
collection PubMed
description Collision cross-section (CCS) measurements obtained from ion mobility spectrometry-mass spectrometry (IMS-MS) analyses often provide useful information concerning a protein’s size and shape and can be complemented by modeling procedures. However, there have been some concerns about the extent to which certain proteins maintain a native-like conformation during the gas-phase analysis, especially proteins with dynamic or extended regions. Here we have measured the CCSs of a range of biomolecules including non-globular proteins and RNAs of different sequence, size, and stability. Using traveling wave IMS-MS, we show that for the proteins studied, the measured CCS deviates significantly from predicted CCS values based upon currently available structures. The results presented indicate that these proteins collapse to different extents varying on their elongated structures upon transition into the gas-phase. Comparing two RNAs of similar mass but different solution structures, we show that these biomolecules may also be susceptible to gas-phase compaction. Together, the results suggest that caution is needed when predicting structural models based on CCS data for RNAs as well as proteins with non-globular folds. [Figure: see text] ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1007/s13361-017-1689-9) contains supplementary material, which is available to authorized users.
format Online
Article
Text
id pubmed-5556138
institution National Center for Biotechnology Information
language English
publishDate 2017
publisher Springer US
record_format MEDLINE/PubMed
spelling pubmed-55561382017-08-28 Investigating the Structural Compaction of Biomolecules Upon Transition to the Gas-Phase Using ESI-TWIMS-MS Devine, Paul W. A. Fisher, Henry C. Calabrese, Antonio N. Whelan, Fiona Higazi, Daniel R. Potts, Jennifer R. Lowe, David C. Radford, Sheena E. Ashcroft, Alison E. J Am Soc Mass Spectrom Research Article Collision cross-section (CCS) measurements obtained from ion mobility spectrometry-mass spectrometry (IMS-MS) analyses often provide useful information concerning a protein’s size and shape and can be complemented by modeling procedures. However, there have been some concerns about the extent to which certain proteins maintain a native-like conformation during the gas-phase analysis, especially proteins with dynamic or extended regions. Here we have measured the CCSs of a range of biomolecules including non-globular proteins and RNAs of different sequence, size, and stability. Using traveling wave IMS-MS, we show that for the proteins studied, the measured CCS deviates significantly from predicted CCS values based upon currently available structures. The results presented indicate that these proteins collapse to different extents varying on their elongated structures upon transition into the gas-phase. Comparing two RNAs of similar mass but different solution structures, we show that these biomolecules may also be susceptible to gas-phase compaction. Together, the results suggest that caution is needed when predicting structural models based on CCS data for RNAs as well as proteins with non-globular folds. [Figure: see text] ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1007/s13361-017-1689-9) contains supplementary material, which is available to authorized users. Springer US 2017-05-08 2017 /pmc/articles/PMC5556138/ /pubmed/28484973 http://dx.doi.org/10.1007/s13361-017-1689-9 Text en © The Author(s) 2017 Open Access This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
spellingShingle Research Article
Devine, Paul W. A.
Fisher, Henry C.
Calabrese, Antonio N.
Whelan, Fiona
Higazi, Daniel R.
Potts, Jennifer R.
Lowe, David C.
Radford, Sheena E.
Ashcroft, Alison E.
Investigating the Structural Compaction of Biomolecules Upon Transition to the Gas-Phase Using ESI-TWIMS-MS
title Investigating the Structural Compaction of Biomolecules Upon Transition to the Gas-Phase Using ESI-TWIMS-MS
title_full Investigating the Structural Compaction of Biomolecules Upon Transition to the Gas-Phase Using ESI-TWIMS-MS
title_fullStr Investigating the Structural Compaction of Biomolecules Upon Transition to the Gas-Phase Using ESI-TWIMS-MS
title_full_unstemmed Investigating the Structural Compaction of Biomolecules Upon Transition to the Gas-Phase Using ESI-TWIMS-MS
title_short Investigating the Structural Compaction of Biomolecules Upon Transition to the Gas-Phase Using ESI-TWIMS-MS
title_sort investigating the structural compaction of biomolecules upon transition to the gas-phase using esi-twims-ms
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5556138/
https://www.ncbi.nlm.nih.gov/pubmed/28484973
http://dx.doi.org/10.1007/s13361-017-1689-9
work_keys_str_mv AT devinepaulwa investigatingthestructuralcompactionofbiomoleculesupontransitiontothegasphaseusingesitwimsms
AT fisherhenryc investigatingthestructuralcompactionofbiomoleculesupontransitiontothegasphaseusingesitwimsms
AT calabreseantonion investigatingthestructuralcompactionofbiomoleculesupontransitiontothegasphaseusingesitwimsms
AT whelanfiona investigatingthestructuralcompactionofbiomoleculesupontransitiontothegasphaseusingesitwimsms
AT higazidanielr investigatingthestructuralcompactionofbiomoleculesupontransitiontothegasphaseusingesitwimsms
AT pottsjenniferr investigatingthestructuralcompactionofbiomoleculesupontransitiontothegasphaseusingesitwimsms
AT lowedavidc investigatingthestructuralcompactionofbiomoleculesupontransitiontothegasphaseusingesitwimsms
AT radfordsheenae investigatingthestructuralcompactionofbiomoleculesupontransitiontothegasphaseusingesitwimsms
AT ashcroftalisone investigatingthestructuralcompactionofbiomoleculesupontransitiontothegasphaseusingesitwimsms