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Kevin Pagel

Kevin Pagel

Freie Universität Berlin
Germany

Overview

What is he best known for?

The fields of study he is best known for:

  • Organic chemistry
  • Biochemistry
  • Amino acid

His primary areas of study are Mass spectrometry, Ion-mobility spectrometry, Analytical chemistry, Ion and Protein folding. His Mass spectrometry study frequently draws connections between adjacent fields such as Glycan. His Ion-mobility spectrometry research integrates issues from Carbohydrate synthesis, Nuclear magnetic resonance spectroscopy of carbohydrates and Stereoisomerism.

His Infrared spectroscopy study in the realm of Analytical chemistry interacts with subjects such as Tandem. His studies in Infrared spectroscopy integrate themes in fields like Crystallography, van der Waals force, Protein secondary structure and Density functional theory. His Protein folding study combines topics in areas such as Chemical physics, Biophysics and Protein structure, Beta sheet, Peptide.

His most cited work include:

  • Identification of carbohydrate anomers using ion mobility–mass spectrometry (158 citations)
  • Identification of carbohydrate anomers using ion mobility–mass spectrometry (158 citations)
  • Alternate Dissociation Pathways Identified in Charge-Reduced Protein Complex Ions (105 citations)

What are the main themes of his work throughout his whole career to date?

Mass spectrometry, Infrared spectroscopy, Ion, Ion-mobility spectrometry and Crystallography are his primary areas of study. The Mass spectrometry study combines topics in areas such as Stereochemistry, Dissociation and Glycan. The study incorporates disciplines such as Glycosyl, Computational chemistry and Hydrogen bond in addition to Infrared spectroscopy.

His research integrates issues of Characterization, Protein tertiary structure and Monosaccharide in his study of Ion. Kevin Pagel studied Ion-mobility spectrometry and Molecule that intersect with Photochemistry. His Crystallography research incorporates themes from Solvent, Protein secondary structure, Protein structure, Conformational isomerism and Peptide.

He most often published in these fields:

  • Mass spectrometry (86.26%)
  • Infrared spectroscopy (49.45%)
  • Ion (41.21%)

What were the highlights of his more recent work (between 2020-2021)?

  • Infrared spectroscopy (49.45%)
  • Mass spectrometry (86.26%)
  • Glycan (32.97%)

In recent papers he was focusing on the following fields of study:

His main research concerns Infrared spectroscopy, Mass spectrometry, Glycan, Computational chemistry and Chondroitin sulfate. His work carried out in the field of Infrared spectroscopy brings together such families of science as Supramolecular chemistry, Chemical physics, Characterization, Crown ether and Azobenzene. His study of Ion-mobility spectrometry is a part of Mass spectrometry.

To a larger extent, Kevin Pagel studies Ion with the aim of understanding Ion-mobility spectrometry. He has researched Glycan in several fields, including Nuclear magnetic resonance spectroscopy, Electrospray ionization and Protein secondary structure. His studies deal with areas such as Crystallography, Disaccharide, Lipid monolayer and Chondroitin as well as Chondroitin sulfate.

Between 2020 and 2021, his most popular works were:

  • Unravelling the structural complexity of glycolipids with cryogenic infrared spectroscopy (3 citations)
  • Unravelling the structural complexity of glycolipids with cryogenic infrared spectroscopy (3 citations)
  • Chondroitin Sulfate Disaccharides in the Gas Phase: Differentiation and Conformational Constraints. (0 citations)

In his most recent research, the most cited papers focused on:

  • Organic chemistry
  • Biochemistry
  • Amino acid

Kevin Pagel focuses on Computational chemistry, Infrared spectroscopy, Glycan, Characterization and Glycoconjugate. His Glycan study frequently intersects with other fields, such as Disaccharide. His Disaccharide research includes elements of Chondroitin, Dermatan sulfate, Chondroitin sulfate, Sulfation and Macromolecule.

His biological study spans a wide range of topics, including Glycolipid, Glycobiology and Analytical technique.

This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.

Best Publications

Identification of carbohydrate anomers using ion mobility–mass spectrometry

Johanna Hofmann;Johanna Hofmann;H. S. Hahm;P. H. Seeberger;P. H. Seeberger;Kevin Pagel;Kevin Pagel.
Nature (2015)

300 Citations

Recommendations for reporting ion mobility Mass Spectrometry measurements

Valérie Gabelica;Alexandre A. Shvartsburg;Carlos Afonso;Perdita Barran.
Mass Spectrometry Reviews (2019)

254 Citations

Protomers of Benzocaine: Solvent and Permittivity Dependence

Stephan Warnke;Jongcheol Seo;Jasper Boschmans;Frank Sobott.
Journal of the American Chemical Society (2015)

175 Citations

Alternate Dissociation Pathways Identified in Charge-Reduced Protein Complex Ions

Kevin Pagel;Suk Joon Hyung;Brandon T. Ruotolo;Carol V. Robinson.
Analytical Chemistry (2010)

168 Citations

An infrared spectroscopy approach to follow β-sheet formation in peptide amyloid assemblies

Jongcheol Seo;Waldemar Hoffmann;Waldemar Hoffmann;Stephan Warnke;Xing Huang.
Nature Chemistry (2017)

158 Citations

Ion Mobility–Mass Spectrometry of Complex Carbohydrates: Collision Cross Sections of Sodiated N-linked Glycans

Kevin Pagel;David J. Harvey;David J. Harvey.
Analytical Chemistry (2013)

133 Citations

Random Coils, β-Sheet Ribbons, and α-Helical Fibers: One Peptide Adopting Three Different Secondary Structures at Will

Kevin Pagel;Sara C Wagner;Kerim Samedov;Hans von Berlepsch.
Journal of the American Chemical Society (2006)

116 Citations

Retention of Native Protein Structures in the Absence of Solvent: A Coupled Ion Mobility and Spectroscopic Study.

Jongcheol Seo;Waldemar Hoffmann;Stephan Warnke;Michael T. Bowers.
Angewandte Chemie (2016)

111 Citations

Glycan Analysis by Ion Mobility-Mass Spectrometry

Johanna Hofmann;Kevin Pagel.
Angewandte Chemie (2017)

106 Citations

Secondary structure of Ac-Ala$_n$-LysH$^+$ polyalanine peptides ($n$=5,10,15) in vacuo: Helical or not?

M. Rossi;V. Blum;P. Kupser;G. von Helden.
arXiv: Biological Physics (2010)

104 Citations

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