J
Jiří Kessler
Researcher at Academy of Sciences of the Czech Republic
Publications - 26
Citations - 489
Jiří Kessler is an academic researcher from Academy of Sciences of the Czech Republic. The author has contributed to research in topics: Raman optical activity & Circular dichroism. The author has an hindex of 11, co-authored 26 publications receiving 362 citations. Previous affiliations of Jiří Kessler include Institute of Chemical Technology in Prague & Charles University in Prague.
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Recent Trends in Chiroptical Spectroscopy: Theory and Applications of Vibrational Circular Dichroism and Raman Optical Activity
TL;DR: New chiroptical phenomena have been observed, such as enhanced circular dichroism of biopolymers (protein fibrils, nucleic acids), plasmonic and resonance chirality-transfer ROA experiments, and some of them are not yet understood or attributed to instrumental artifacts so far.
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First-Principles Predictions of Vibrational Raman Optical Activity of Globular Proteins
TL;DR: In this article, the authors obtained a stunning agreement between experimental and theoretical vibrational spectra of large globular proteins containing thousands of atoms as well, revealing a wealth of information, such as the nature of localized molecular motions as well as collective vibrational modes describing folding of larger protein parts.
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Detection of Sugars via Chirality Induced in Europium(III) Compounds
Tao Wu,Jiří Průša,Jiří Průša,Jiří Kessler,Jiří Kessler,Martin Dračínský,Jan Valenta,Petr Bouř +7 more
TL;DR: The present study shows that circularly polarized luminescence (CPL) induced in europium complexes provides very specific spectral patterns for fructose, mannose, glucose, and galactose, which appear to be convenient means for monosaccharide detection and identification.
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Insight into vibrational circular dichroism of proteins by density functional modeling.
TL;DR: The Cartesian-coordinate based tensor transfer is applied making it possible to extend the density functional theory (DFT) and model spectral intensities of large globular proteins nearly at quantum-chemical precision and revealed which structural information can (and cannot) be obtained from this kind of spectroscopy.
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Chiral sensing of amino acids and proteins chelating with Eu(III) complexes by Raman optical activity spectroscopy.
Tao Wu,Jiří Kessler,Petr Bouř +2 more
TL;DR: Circularly polarized luminescence (CPL) of a europium complex induced by amino acids is monitored by Raman optical activity (ROA) spectroscopy, which enables us to detect weak CPL bands invisible to conventional CPL spectrometers.