T
Tore Brinck
Researcher at Royal Institute of Technology
Publications - 160
Citations - 8964
Tore Brinck is an academic researcher from Royal Institute of Technology. The author has contributed to research in topics: Catalysis & Ab initio. The author has an hindex of 47, co-authored 158 publications receiving 8104 citations. Previous affiliations of Tore Brinck include University of New Orleans.
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Quantitative analysis of molecular surfaces: areas, volumes, electrostatic potentials and average local ionization energies
TL;DR: This work describes a procedure for performing quantitative analyses of fields f(r) on molecular surfaces, including statistical quantities and locating and evaluating their local extrema, based on the very popular representation of a surface as collection of polygons.
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Tuning the HOMO and LUMO energy levels of organic chromophores for dye sensitized solar cells.
Daniel P. Hagberg,Tannia Marinado,Karl Martin Karlsson,Kazuteru Nonomura,Peng Qin,Gerrit Boschloo,Tore Brinck,Anders Hagfeldt,Licheng Sun +8 more
TL;DR: Results show that energetic tuning of the chromophores was successful and fulfilled the thermodynamic criteria for dye-sensitized solar cells, electrical losses depending on the size and orientation of the Chromophores were observed.
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Surface electrostatic potentials of halogenated methanes as indicators of directional intermolecular interactions
TL;DR: In this article, the authors used an ab initio self-consistent field molecular orbital approach to compute 6-31G*/STO-3G* electrostatic potentials for CH3F, CF4, CH3Cl, CCl4, C3Br, and CBr4.
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Average local ionization energies on the molecular surfaces of aromatic systems as guides to chemical reactivity
TL;DR: In this paper, the average ionization energy (AIE) was introduced and used as a guide to chemical reactivity in aromatic systems, which is rigorously defined within the framework of self-consistent-...
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Carbon-Carbon Bonds by Hydrolytic Enzymes
TL;DR: Ser105 in CALB was targeted by site-directed mutagenesis to create enzyme variants lacking the nucleophilic feature of the active site, and it is expected that the new catalytic activity, harbored in the stable protein scaffold of the lipase, will allow aldol additions of substrates, which cannot be reached by traditional aldlases.