Biomedical subjects

E Michalski

Publications and source records attributed to E Michalski.

At least 19 recordsLinked to original sources

PubMed2006

UV-induced nonlinear absorption in lanthanum calcium borate single crystals.

It has been revealed that lanthanum calcium borate (La2CaB10O19) crystals show two-photon absorption (TPA) induced by a UV laser field. UV-induced TPA measurements were performed in the spectral range of 475-1130 nm using as fundamental beam the third harmonics of the 28 ps Nd-YAG pulsed laser as a pumping beam for LiB3O5 optical parametrized generator using Z-scan method. Investigations performed by the Z-scan method were done during illumination by a Xe-F laser (lambda = 217 nm) as a photoinducing (pumping) beam. The pumping laser beam created a thin surface layer (about 80-90 nm) that was the source of the observed photoinduced TPA. The highest values of the TPA beta coefficients were achieved for polarization of the pumping light directed along the second-order crystallographic axis of the investigated crystals. The obtained values of the TPA coefficients were higher than those for the BiB3O6 crystals investigated earlier by us.

Journal Article↗

PubMed2004

High-average-power femtosecond pulse generation in the blue using BiB3O6.

Efficient generation of tunable femtosecond pulses in the blue is reported in the nonlinear crystal BiB3O6. By use of fundamental pulses from a mode-locked Ti:sapphire laser at 76 MHz, single-pass second-harmonic average powers of as much as 830 mW have been generated at 50% conversion efficiency, and a tunable range of 375-435 nm in the blue is demonstrated. Temporal measurements using cross correlation of the fundamental and second-harmonic pulses in a 100-microm-thick beta-BaB2O4 crystal result in blue pulse durations of 220 fs for 130-fs fundamental pulses. Direct experimental comparison with beta-BaB2O4 confirms the superior performance BiB3O6 for second-harmonic generation of femtosecond pulses.

Journal Article↗

PubMed1997

Inverse sequence similarity in proteins and its relation to the three-dimensional fold.

Nowadays the most successful strategy for the prediction of the tertiary structure of proteins is the homology-based modelling using known structures. A real chance to predict the general fold of a protein arises only in cases with a sufficient sequence homology (e.g. 27% over 100 residues). In this analysis we examine the phenomenon of inverse sequence similarity (ISS) in proteins and its structural meaning. In sequence data bases we found a lot of examples for ISS up to 34% identity over 204 residues and a surprisingly large number of self-inverse protein sequences. By inspection of inverse similar sequence pairs with known tertiary structures we observe that inverse sequence alignments above the threshold indicating structural similarity generally do not imply comparable folds for both. From our analysis we conclude that the straightforward employment of ISS for protein structure prediction fails even above the known threshold for 'safe similarity'.

Amino Acid Sequence↗

PubMed1981