Browsing Chemistry and Biochemistry by Author "Jensen, Ole N."

Now showing items 1-5 of 5

    • 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) ...

    • 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 ...

    • 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 ...

    • 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 ...

    • Top-down ion mobility separations of isomeric proteoforms 

      Berthias, Francis; Thurman, Hayden A.; Wijegunawardena, Gayani; Wu, Haifan; Shvartsburg, Alexandre A.; Jensen, Ole N. (American Chemical Society, 2022-12-23)
      Continuing advances in proteomics highlight the ubiquity and biological importance of proteoforms proteins with varied sequence, splicing, or distribution of post-translational modifications (PTMs). The preeminent example ...