Koit Mauring
University of Tartu
17 Papers
65 Citations
Koit Mauring is an academic researcher from University of Tartu. The author has contributed to research in topics: Fluorescence spectroscopy & Light beam. The author has an hindex of 8, co-authored 17 publications.
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Papers
Spectral shift mechanisms of chlorophylls in liquids and proteins.
Indrek Renge,Koit Mauring +1 more
TL;DR: Non-excitonic spectral shifts of chlorophylls that can reach -1,000 cm(-1) in pigment-protein complexes are investigated, basing on absorption and fluorescence measurements in large number of liquids.
41
Control of the blue fluorescent protein with advanced evolutionary pulse shaping.
Eric R. Tkaczyk,Koit Mauring,Alan H. Tkaczyk,Alan H. Tkaczyk,V. Krasnenko,Jing Yong Ye,James R. Baker,Theodore B. Norris +7 more
TL;DR: Using a genetic algorithm with a multiplicative (rather than ratiometric) fitness parameter, this work is able to control the ratio of BFP fluorescence to second-harmonic generation without a considerable drop in the maximized signal.
15
Control of two-photon fluorescence of common dyes and conjugated dyes.
Eric R. Tkaczyk,Alan H. Tkaczyk,Alan H. Tkaczyk,Koit Mauring,Jing Yong Ye,James R. Baker,Theodore B. Norris +6 more
TL;DR: The results show that the ability to discriminate dyes is determined almost entirely by their differences in two-photon excitation cross section, and the results are compared to a quantitative measure of the noise level.
13
Energy Selection Is Not Correlated in the Qx and Qy Bands of a Mg-Porphyrin Embedded in a Protein
TL;DR: The Qx-Qy splitting observed in the fluorescence excitation spectra of Mg-mesoporphyrin-IX substituted horseradish peroxidase and of its complex with naphthohydroxamic acid was studied by spectral hole burning techniques and showed a clear lack of correlation between the electronic transition energies of the Qx and Qy bands.
10
Physicochemical properties of blue fluorescent protein determined via molecular dynamics simulation
TL;DR: It is shown that decreased temperature as well as applied pressure increases the water viscosity, but the concomitant decrease of the BFP diffusion coefficient behaves differently from Stokes-Einstein formula, and the number of hydrogen bonds around the protein grows with pressure, which explains the aforementioned deviation.