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Sebastian Schlücker

Researcher at University of Duisburg-Essen

Publications -  188
Citations -  10165

Sebastian Schlücker is an academic researcher from University of Duisburg-Essen. The author has contributed to research in topics: Raman spectroscopy & Raman scattering. The author has an hindex of 40, co-authored 176 publications receiving 7639 citations. Previous affiliations of Sebastian Schlücker include University of Osnabrück & University of Würzburg.

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Tunable optical setup with high flexibility for spectrally resolved coherent anti-Stokes Raman scattering microscopy

TL;DR: In this paper, a simplified setup for coherent anti-Stokes Raman scattering (CARS) microscopy is introduced, which allows for recording CARS images with 30 cm-1 excitation bandwidth for probing Raman bands between 500 and 900 cm 1 with minimal requirements for alignment.
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UV resonance Raman spectroscopic monitoring of supramolecular complex formation: peptide recognition in aqueous solution

TL;DR: The formation of a supramolecular complex between a tetrapeptide and an artificial receptor, which is monitored at submillimolar concentrations in water by UV resonance Raman spectroscopy, is monitored using 275 nm excitation to selectively probe the carboxylate binding site within the receptor.
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Label-free SERS monitoring of hydride reduction catalyzed by Au nanostars

TL;DR: In this paper, the surface-enhanced Raman scattering (SERS) is used to study chemical reactions catalyzed by nobel metal nanoparticles, and a simple two-step route is developed to demonstrate shape-controlled synthesis and morphology-dependent catalytic activity of AuNSs.
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Characterization of guanidiniocarbonyl pyrroles in water by pH-dependent UV Raman spectroscopy and component analysis

TL;DR: A pH-dependent UV RR spectroscopic investigation of two guanidiniocarbonyl pyrroles in water is presented and the small model receptor CBS-NH2 and the larger peptide receptors CBS-Lys- Lys-Phe- NH2 can both be described as linear combinations of only two components.
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Site-specific pKa determination of the carboxylate-binding subunit in artificial peptide receptors

TL;DR: Site-specific pK(a) determination of the carboxylate-binding subunit in artificial peptide receptors is achieved by pH-dependent UV resonance Raman scattering with subsequent matrix factorization.