Travelling wave ion mobility mass spectrometry studies of protein structure

Biological significance and comparison with X-ray crystallography and nuclear magnetic resonance spectroscopy measurements

Charlotte A. Scarff, Konstantinos Thalassinos, Gillian R. Hilton, James Scrivens

Research output: Contribution to journalArticleResearchpeer-review

119 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)3297-3304
Number of pages8
JournalRapid Communications in Mass Spectrometry
Volume22
Issue number20
DOIs
Publication statusPublished - 30 Oct 2008

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X ray crystallography
Nuclear magnetic resonance spectroscopy
Mass spectrometry
Ions
Proteins
Gases
Conformations
Phase structure
Nuclear magnetic resonance
X rays

Cite this

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title = "Travelling wave ion mobility mass spectrometry studies of protein structure: Biological significance and comparison with X-ray crystallography and nuclear magnetic resonance spectroscopy measurements",
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.",
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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. / Scarff, Charlotte A.; Thalassinos, Konstantinos; Hilton, Gillian R.; Scrivens, James .

In: Rapid Communications in Mass Spectrometry, Vol. 22, No. 20, 30.10.2008, p. 3297-3304.

Research output: Contribution to journalArticleResearchpeer-review

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