Browsing CHEM Faculty Scholarship by Author "Baird, Matthew A."
Now showing items 1-13 of 13
-
Characterization of complete histone tail proteoforms using differential ion mobility spectrometry
Shliaha, Pavel V.; Baird, Matthew A.; Nielsen, Mogens M.; Gorshkov, Vladimir A.; Bowman, Andrew P.; Kaszycki, Julia L.; Jensen, Ole N.; Shvartsburg, Alexandre A. (American Chemical Society, 2017-05-16)Histone proteins are subject to dynamic post-translational modifications (PTMs) that cooperatively modulate the chromatin structure and function. Nearly all functional PTMs are found on the N-terminal histone domains (tails) ... -
Delineation of Isomers by the 13C Shifts in Ion Mobility Spectra
Pathak, Pratima; Sarycheva, Anastasia; Baird, Matthew A.; Shvartsburg, Alexandre A. (American Chemical Society, 2020-11-17)Mass spectrometry (MS) and isotopes were intertwined for a century, with stable isotopes central to many MS identification and quantification protocols. In contrast, the analytical separations including ion mobility ... -
Differential ion mobility separations/mass spectrometry with high resolution in both dimensions
Baird, Matthew A.; Anderson, Gordon A.; Shliaha, Pavel V.; Jensen, Ole Noerregaard; Shvartsburg, Alexandre A. (American Chemical Society, 2019-01-15)Strong orthogonality to mass spectrometry makes differential ion mobility spectrometry (FAIMS) a powerful tool for isomer separations. However, high FAIMS resolution has been achieved overall only with buffers rich in He ... -
Elemental dependence of structurally specific isotopic shifts in high-field ion mobility spectra
Baird, Matthew A.; Pathak, Pratima; Shvartsburg, Alexandre A. (ACS, 2019-02-01)Nearly all molecules incorporate at least one element with stable isotopes, yielding ubiquitous isotopologic envelopes in mass spectra. Those envelopes split in differential or field asymmetric waveform ion mobility (FAIMS) ... -
Fast and effective ion mobility-mass spectrometry separation of D-amino-acid-containing peptides
Fouque, Kevin Jeanne Dit; Garabedian, Alyssa; Porter, Jacob; Baird, Matthew A.; Pang, Xueqin; Williams, Todd D.; Li, Lingjun; Shvartsburg, Alexandre A.; Fernandez-Lima, Francisco (American Chemical Society, 2017-11-01)Despite often minute concentrations in vivo, d-amino acid containing peptides (DAACPs) are crucial to many life processes. Standard proteomics protocols fail to detect them as d/l substitutions do not affect the peptide ... -
High-resolution differential ion mobility separations/orbitrap mass spectrometry without buffer gas limitations
Baird, Matthew A.; Shliaha, Pavel V.; Anderson, Gordon A.; Moskovets, Eugene; Laiko, Victor; Makarov, Alexander A.; Jensen, Ole N.; Shvartsburg, Alexandre A. (American Chemical Society, 2019-04-29)Strong orthogonality between differential ion mobility spectrometry (FAIMS) and mass spectrometry (MS) makes their hybrid a powerful approach to separate isomers and isobars. Harnessing that power depends on high resolution ... -
High-resolution ion mobility separations of isomeric glycoforms with variations on the peptide and glycan levels
Pathak, Pratima; Baird, Matthew A.; Shvartsburg, Alexandre A. (American Chemical Society, 2020-06-05)Glycosylation is a ubiquitous post-translational modification (PTM) that strongly affects the protein folding and function. Glycosylation patterns are impacted by many diseases, making promising biomarkers. Glycans are ... -
Identification of isomers by multidimensional isotopic shifts in high-field ion mobility spectra
Pathak, Pratima; Baird, Matthew A.; Shvartsburg, Alexandre A. (American Chemical Society, 2018-07-03)Nearly all molecules incorporate elements with stable isotopes. The resulting isotopologue envelopes in mass spectra tell the exact stoichiometry but nothing about the geometry. Chromatography and electrophoresis at high ... -
Linear and differential ion mobility separations of middle-down proteoforms
Garabedian, Alyssa; Baird, Matthew A.; Porter, Jacob; Fouque, Kevin Jeanne Dit; Shliaha, Pavel V.; Jensen, Ole N.; Williams, Todd D.; Fernandez-Lima, Francisco; Shvartsburg, Alexandre A. (American Chemical Society, 2018)Comprehensive characterization of proteomes comprising the same proteins with distinct post-translational modifications (PTMs) is a staggering challenge. Many such proteoforms are isomers (localization variants) that require ... -
Localization of post-translational modifications in peptide mixtures via high-resolution differential ion mobility separations followed by electron transfer dissociation
Baird, Matthew A.; Shvartsburg, Alexandre A. (Springer International Publishing, 2016-12)Precise localization of post-translational modifications (PTMs) on proteins and peptides is an outstanding challenge in proteomics. While electron transfer dissociation (ETD) has dramatically advanced PTM analyses, mixtures ... -
Middle-down proteomic analyses with Ion mobility separations of endogenous isomeric proteoforms
Shliaha, Pavel V.; Gorshkov, Vladimir A.; Kovalchuk, Sergey I.; Schwammle, Veit; Baird, Matthew A.; Shvartsburg, Alexandre A.; Jensen, Ole N. (NLM (Medline), 2020-01-14)Biological functions of many proteins are governed by post-translational modifications (PTMs). In particular, the rich PTM complement in histones controls the gene expression and chromatin structure with major health ... -
Molecular structure characterization by isotopic splitting in nonlinear ion mobility spectra
Kaszycki, Julia L.; Baird, Matthew A.; Shvartsburg, Alexandre A. (American Chemical Society, 2018-01-02)Nearly all compounds comprise numerous isotopologues ensuing from stable natural isotopes for constituent elements. The consequent isotopic envelopes in mass spectra can reveal the ion stoichiometry but not geometry. We ... -
Structurally informative isotopic shifts in ion mobility spectra for heavier species
Pathak, Pratima; Baird, Matthew A.; Shvartsburg, Alexandre A. (American Chemical Society, 2019-11-20)The isotopic molecular envelopes due to stable isotopes for most elements were a staple of mass spectrometry since its origins, often leveraged to identify and quantify compounds. However, all isomers share one MS envelope. ...