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Matthew S. Glover

Researcher at Indiana University

Publications -  26
Citations -  756

Matthew S. Glover is an academic researcher from Indiana University. The author has contributed to research in topics: Peptide & Mass spectrometry. The author has an hindex of 14, co-authored 23 publications receiving 639 citations. Previous affiliations of Matthew S. Glover include University of Wisconsin-Madison & AstraZeneca.

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Electron-Transfer/Higher-Energy Collision Dissociation (EThcD)-Enabled Intact Glycopeptide/Glycoproteome Characterization

TL;DR: A redefined electron-transfer/higher-energy collision dissociation (EThcD) fragmentation scheme is applied to incorporate both glycan and peptide fragments in one single spectrum, enabling complete information to be gathered and great microheterogeneity details to be revealed.
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Hybrid ion mobility and mass spectrometry as a separation tool.

TL;DR: The multitude of ion mobility techniques hybridized to different mass spectrometers are explored, detailing current challenges and opportunities for each ion mobility technique and for what experiments one technique might be chosen over another.
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Infrared Spectroscopy of Mobility-Selected H+-Gly-Pro-Gly-Gly (GPGG)

TL;DR: Ion mobility and spectroscopic data combined with density functional theory (DFT) based molecular dynamics simulations confirm the presence of one major conformer per family, which arises from cis/trans isomerization about the proline residue.
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Recent advances in ion mobility-mass spectrometry for improved structural characterization of glycans and glycoconjugates.

TL;DR: Recent improvements in IM-MS instrumentation and methods for the structural characterization of isomeric glycans are presented, highlighting the enormous potential of this technology in a variety of research areas, including glycomics, glycoproteomics, and glycobiology.
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Using ion mobility data to improve peptide identification: intrinsic amino acid size parameters.

TL;DR: A new method that employs intrinsic amino acid size parameters to obtain ion mobility predictions that can be used to rank candidate peptide ion assignments is proposed.