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Travelling wave ion mobility mass spectrometry studies of protein structure : biological significance and comparison with X-ray crystallography and nuclear magnetic resonance spectroscopy measurements
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Scarff, Charlotte A., Thalassinos, Konstantinos, Hilton, Gillian R. and Scrivens, James H. (2008) Travelling wave ion mobility mass spectrometry studies of protein structure : biological significance and comparison with X-ray crystallography and nuclear magnetic resonance spectroscopy measurements. Rapid Communications in Mass Spectrometry, Vol.22 (No.20). pp. 3297-3304. doi:10.1002/rcm.3737 ISSN 0951-4198.
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Official URL: http://dx.doi.org/10.1002/rcm.3737
Abstract
The three-dimensional conformation of a protein is central to its biological function. The characterisation of aspects of three-dimensional protein structure by mass spectrometry is an area of much interest as the gas-phase conformation, in many instances, can be related to that of the solution phase. Travelling wave ion mobility mass spectrometry (TWIMS) was used to investigate the biological significance of gas-phase protein structure. Protein standards were analysed by TWIMS under denaturing and near-physiological solvent conditions and cross-sections estimated for the charge states observed. Estimates of collision cross-sections were obtained with reference to known standards with published cross-sections. Estimated cross-sections were compared with values from published X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy structures. The cross-section measured by ion mobility mass spectrometry varies with charge state, allowing the unfolding transition of proteins in the gas phase to be studied. Cross-sections estimated experimentally for proteins studied, for charge states most indicative of native structure, are in good agreement with measurements calculated from published X-ray and NMR structures. The relative stability of gas-phase structures has been investigated, for the proteins studied, based on their change in cross-section with increase in charge. These results illustrate that the TWIMS approach can provide data on three-dimensional protein structures of biological relevance. Copyright (C) 2008 John Wiley & Sons, Ltd.
Item Type: | Journal Article | ||||
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Subjects: | Q Science > QD Chemistry Q Science > QC Physics |
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Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) | ||||
Library of Congress Subject Headings (LCSH): | Proteins -- Structure, Ion mobility spectroscopy, Mass spectrometry, X-ray crystallography, Nuclear magnetic resonance spectroscopy | ||||
Journal or Publication Title: | Rapid Communications in Mass Spectrometry | ||||
Publisher: | John Wiley & Sons Ltd. | ||||
ISSN: | 0951-4198 | ||||
Official Date: | October 2008 | ||||
Dates: |
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Volume: | Vol.22 | ||||
Number: | No.20 | ||||
Number of Pages: | 8 | ||||
Page Range: | pp. 3297-3304 | ||||
DOI: | 10.1002/rcm.3737 | ||||
Status: | Peer Reviewed | ||||
Publication Status: | Published | ||||
Access rights to Published version: | Restricted or Subscription Access |
Data sourced from Thomson Reuters' Web of Knowledge
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