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dc.contributor.authorShvartsburg, Alexandre A.
dc.date.accessioned2014-12-16T03:05:28Z
dc.date.available2014-12-16T03:05:28Z
dc.date.issued2014-11-04
dc.identifier.citationShvartsburg, Alexandre A. 2014. Ultrahigh-resolution differential ion mobility separations of conformers for proteins above 10 kDa: onset of dipole alignment? Analytical Chemistry 2014 86 (21), 10608-10615en_US
dc.identifier.issn0003-2700
dc.identifier.otherWOS:000344510200018
dc.identifier.urihttp://dx.doi.org/10.1021/ac502389a
dc.identifier.urihttp://hdl.handle.net/10057/11016
dc.descriptionClick on the DOI link to access the article (may not be free).en_US
dc.description.abstractBiomacromolecules tend to assume numerous structures in solution or the gas phase. It has been possible to resolve disparate conformational families but not unique geometries within each, and drastic peak broadening has been the bane of protein analyses by chromatography, electrophoresis, and ion mobility spectrometry (IMS). The new differential or field asymmetric waveform IMS (FAIMS) approach using hydrogen-rich gases was recently found to separate conformers of a small protein ubiquitin with the same peak width and resolving power up to similar to 400 as for peptides. The present work explores the reach of this approach for larger proteins, exemplified by cytochrome c and myoglobin. Resolution similar to that for ubiquitin was largely achieved with longer separations, while the onset of peak broadening and coalescence with shorter separations suggests the limitation of the present technique to proteins under similar to 20 kDa. This capability may enable one to distinguish whole proteins with differing residue sequences or localizations of post-translational modifications. Small features at negative compensation voltages that markedly grow from cytochrome c to myoglobin indicate the dipole alignment of rare conformers in accord with theory, further supporting the concept of pendular macroions in FAIMS.en_US
dc.description.sponsorshipThis work was funded by the PNNL Technology Commercialization Office and Laboratory-Directed Research & Development program and carried out in the Environmental Molecular Sciences Laboratory, a DOE national scientific user facility at PNNL.en_US
dc.language.isoen_USen_US
dc.publisherAmerican Chemical Societyen_US
dc.relation.ispartofseriesAnalytical Chemistry;v.86:no.21
dc.subjectMolecular-dynamics simulationsen_US
dc.subjectUnsolvated cytochrome-cen_US
dc.subjectEsi-faims-msen_US
dc.subjectGas-phaseen_US
dc.subjectMass-spectrometryen_US
dc.subjectLiquid-chromatographyen_US
dc.subjectCross-sectionsen_US
dc.subjectHistone codeen_US
dc.subjectIn-vacuoen_US
dc.subjectConformationsen_US
dc.titleUltrahigh-resolution differential ion mobility separations of conformers for proteins above 10 kDa: onset of dipole alignment?en_US
dc.typeArticleen_US
dc.rights.holderCopyright © 2014 American Chemical Society


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