Magnifying ion mobility spectrometry–mass spectrometry measurements for biomolecular structure studies

Magnifying ion mobility spectrometry–mass spectrometry measurements for biomolecular structure... Available online at www.sciencedirect.com ScienceDirect Magnifying ion mobility spectrometry–mass spectrometry measurements for biomolecular structure studies Sandra N Majuta, Hossein Maleki, Ahmad Kiani Karanji, Kushani Attanyake, Elinore Loch and Stephen J Valentine The variables in Eq. (1) include: ion charge (ze), the Ion mobility spectrometry–mass spectrometry (IMS–MS) Boltzmann constant (k ), the reduced masses of the ion provides information about the structures of gas-phase ions in and the buffer gas (m and m ), the length of the drift tube the form of a collision cross section (CCS) with a neutral buffer I B gas. Indicating relative ion size, a CCS value alone is of limited (L), the pressure and temperature of the buffer gas (T and utility. Although such information can be used to propose P), and the neutral number density at STP (N). Essen- different conformer types, finer details of structure are not tially, from Eq. (1), biomolecular ion size differentiation captured. The increased accessibility of IMS–MS becomes apparent because ions of a larger physical size measurements with commercial instrumentation in recent experience a greater number of collisions with the buffer years has ballooned its usage in combination with separate gas in the drift tube thus increasing t http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Current Opinion in Chemical Biology Elsevier

Magnifying ion mobility spectrometry–mass spectrometry measurements for biomolecular structure studies

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Publisher
Elsevier
Copyright
Copyright © 2017 Elsevier Ltd
ISSN
1367-5931
D.O.I.
10.1016/j.cbpa.2017.11.013
Publisher site
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Abstract

Available online at www.sciencedirect.com ScienceDirect Magnifying ion mobility spectrometry–mass spectrometry measurements for biomolecular structure studies Sandra N Majuta, Hossein Maleki, Ahmad Kiani Karanji, Kushani Attanyake, Elinore Loch and Stephen J Valentine The variables in Eq. (1) include: ion charge (ze), the Ion mobility spectrometry–mass spectrometry (IMS–MS) Boltzmann constant (k ), the reduced masses of the ion provides information about the structures of gas-phase ions in and the buffer gas (m and m ), the length of the drift tube the form of a collision cross section (CCS) with a neutral buffer I B gas. Indicating relative ion size, a CCS value alone is of limited (L), the pressure and temperature of the buffer gas (T and utility. Although such information can be used to propose P), and the neutral number density at STP (N). Essen- different conformer types, finer details of structure are not tially, from Eq. (1), biomolecular ion size differentiation captured. The increased accessibility of IMS–MS becomes apparent because ions of a larger physical size measurements with commercial instrumentation in recent experience a greater number of collisions with the buffer years has ballooned its usage in combination with separate gas in the drift tube thus increasing t

Journal

Current Opinion in Chemical BiologyElsevier

Published: Feb 1, 2018

References

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