Open AccessDenaturation of proteins with beta-barrel topology induced by guanidine hydrochloride
Author(s) -
Olesya V. Stepanenko,
Irina М. Kuznetsova,
Vladislav V. Verkhusha,
Maria Staiano,
Sabato D’Auria,
Konstantin К. Turoverov
Publication year - 2010
Publication title -
spectroscopy an international journal
Language(s) - English
Resource type - Journals
eISSN - 1875-922X
pISSN - 0712-4813
DOI - 10.1155/2010/935656
Subject(s) - guanidine , globular protein , chemistry , chromophore , hydrochloride , biophysics , fluorescence , green fluorescent protein , denaturation (fissile materials) , tryptophan , planarity testing , barrel (horology) , topology (electrical circuits) , crystallography , stereochemistry , biochemistry , amino acid , organic chemistry , biology , materials science , nuclear chemistry , physics , mathematics , quantum mechanics , combinatorics , gene , composite material
The stability of the representatives of two protein classes with β -barrel topology: porcine odorant-binding protein (OBP) and a number of fluorescent proteins (FPs), was studied. It was shown that both of them are significantly more stable than globular α-helical and α / β proteins. At the same time the value of energy barrier between native and unfolded state for FPs exceeds that for OBP. It was found that the small guanidine hydrochloride concentrations induce local structural disturbances in proteins: changes in microenvironment of tryptophan residue in the case of odorant-binding protein and decrease in chromophore non-planarity in the case of green fluorescent protein.
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