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Zsolt Gengeliczki

Researcher at Stanford University

Publications -  23
Citations -  691

Zsolt Gengeliczki is an academic researcher from Stanford University. The author has contributed to research in topics: Ion & Ab initio. The author has an hindex of 15, co-authored 23 publications receiving 645 citations. Previous affiliations of Zsolt Gengeliczki include University of the Pacific (United States) & University of North Carolina at Chapel Hill.

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Imaging photoelectron photoion coincidence spectroscopy with velocity focusing electron optics

TL;DR: An imaging photoelectron photoion coincidence spectrometer at the vacuum ultraviolet (VUV) beamline of the Swiss Light Source is presented and a few initial measurements are reported.
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Structural Dynamics of a Catalytic Monolayer Probed by Ultrafast 2D IR Vibrational Echoes

TL;DR: A method to track fast vibrational motion in solution to probing the interfacial dynamics and structure of a silica surface-tethered transition metal carbonyl complex—tricarbonyl (1,10-phenanthroline)rhenium chloride—of interest as a photoreduction catalyst is extended to catalytically important solid/liquid interfaces.
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Non-standard base pairing and stacked structures in methyl xanthine clusters

TL;DR: In this article, the authors present resonant two-photon ionization and IR-UV double resonance spectra of methylated xanthine derivatives including 7-methylxanthine, theophylline and theobromine monomer, seeded in a supersonic jet by laser desorption.
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IR-UV double resonance spectroscopy of xanthine.

TL;DR: Comparison of the IR-UV double resonance spectrum with frequencies and intensities obtained from density functional theory (DFT) and second order Møller Plesset (MP2) calculations suggests that the observed xanthine is the diketo N(7)H tautomer.
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The Acylaminoacyl Peptidase from Aeropyrum pernix K1 Thought to Be an Exopeptidase Displays Endopeptidase Activity

TL;DR: It is found that the substrate-binding site extends beyond the S2 subsite, being capable of binding peptides with a longer N terminus, which is unique among the enzymes of this family of serine peptidases.