Journal
ANALYTICAL CHEMISTRY
Volume 85, Issue 1, Pages 10-13Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ac3029129
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Funding
- NIH NIGMS [8 P41 GM103493-10]
- U.S. Department of Energy Office of Biological and Environmental Research
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [P41GM103493] Funding Source: NIH RePORTER
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Use of elevated electric fields and helium-rich gases has recently enabled differential ion mobility spectrometry (IMS) with a resolving power up to R 300. Here we applied that technique to a protein (ubiquitin), achieving R up to 80 and separating previously unresolved conformers. While still limited by conformational multiplicity, this resolution is some 4 times greater than that previously reported using either conventional (drift-tube or traveling-wave) or differential IMS. The capability for fine resolution of protein conformers may open new avenues for proteoform separations in top-down and intact-protein proteomics.
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