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Group members






Scientific advisor



Attila Gergely VÉGH

Research associate



Katalin CSONTI

PhD student





The physical basis of protein function

The physical factors behind protein function are the electrostatic interaction between charges and dipoles; electron affinity and the related electron transfer reactions; proton affinity (pK) and the related proton transfer recations as well as hydrogen bonds; steric interactions depending on the 3D protein structure; as well as the interactions with the water molecules inside and around the protein and with the surrounding lipid molecules in case of the membrane proteins. For proteins with chromophoric prostetic groups spectroscopic and kinetic spectroscopic studies in the visible-UV range provide essential information about the protein function. We study the photocycle and the molecular steps of the proton transport in bacterial retinal protein proton pumps, e.g. bacteriorhodopsin, or in signaling proteins, e.g. PYP, and their dependence on environmental factors. We investigate the structural factors affecting the kinetics of electron transfer in cytochromes. We develop and apply general chemometric methods for the analysis of spectral data matrices in order to determine the underlying physical phenomena. In addition, we study the possibilities of the integration of „colored” proteins in biophotonic and in bioelectronic applications.

Biological applications of Scanning Probe and Confocal Raman Microscopy

In our laboratory, we perform structural, morphological and mechanical investigation of biological objects, ranging from proteins up to living cells and tissues. Using atomic force microscopy combined with confocal Raman spectroscopy we try to broaden or knowledge in several biology related areas. Nanometer scale mechanical manipulation and measurement in a liquid environment provides an absolute advantage compared to conventional cellular imaging techniques. Combined with the label-free chemical imaging based on Raman spectroscopy, multiparametric physico-chemical information can be obtained about the studied material. The system serves both collaborative and domestic projects, hence we try to extend our potential towards larger audience. The succesful projects included self assembly of oligonucleotides, structural and morphological studies of nano an microvesicles, mechanical investigation of different bacterial strains, plasticiy of red blood cells, de-adhesion patterns of living brain endothelial cells and last but not least quantitative mapping of several tissues. The above list is far from being complete, it only serves the presentation of the large scale and subject areas where our system can provide valuable information.