scispace - formally typeset
E

Eszter Pongráczné Faragó

Researcher at University of Szeged

Publications -  6
Citations -  132

Eszter Pongráczné Faragó is an academic researcher from University of Szeged. The author has contributed to research in topics: Reaction rate constant & Absorption spectroscopy. The author has an hindex of 4, co-authored 6 publications receiving 112 citations. Previous affiliations of Eszter Pongráczné Faragó include university of lille.

Papers
More filters
Journal ArticleDOI

Rate constant of the reaction between CH3O2 and OH radicals

TL;DR: In this article, the rate constant of the reaction (R1) OH + CH 3 O 2 → products has been measured at 294 k by simultaneous coupling of Laser Induced Fluorescence (LIF) and cw-Cavity Ring Down Spectroscopy (cw-CDRS) to laser photolysis.
Journal ArticleDOI

Absorption Spectrum and Absolute Absorption Cross Sections of CH3O2 Radicals and CH3I Molecules in the Wavelength Range 7473–7497 cm–1

TL;DR: The absorption spectrum of CH3O2 radicals and CH3I molecules has been measured by time-resolved continuous-wave cavity ring-down spectroscopy (cw-CRDS), and three characteristic sharp absorption lines with absorption cross sections up to 2 × 10(-21) cm(2) have been observed in this wavelength range.
Journal ArticleDOI

Experimental determination of the rate constant of the reaction between C2H5O2 and OH radicals

TL;DR: In this article, the rate constant of the reaction C 2 H 5 O 2 + O 2 → products has been measured at T ǫ=296 K using laser photolysis coupled to CRDS and LIF.
Journal ArticleDOI

Critical evaluation of the potential energy surface of the CH3 + HO2reaction system

TL;DR: CHEAT1 protocol based on HEAT345-(Q) method is a robust, general, and cheap alternative for high accurate kinetic calculations, and surpassed the popular standard composite methods.
Journal ArticleDOI

The effect of oxidative stress on the bursopentin peptide structure: A theoretical study

TL;DR: It was discovered that the repulsion between the side chains of Lys(2) and Arg(3) influenced the conformation of the peptide regardless of the configuration of these residues, and Thermodynamic analysis of the epimerisation process showed that the formation of d amino acid residues is favourable.