TY - JOUR
T1 - Denaturation of proteins with beta-barrel topology induced by guanidine hydrochloride
AU - Stepanenko, Olesya V.
AU - Kuznetsova, Irina M.
AU - Verkhusha, Vladislav V.
AU - Staiano, Maria
AU - D'Auria, Sabato
AU - Turoverov, Konstantin K.
PY - 2010
Y1 - 2010
N2 - 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.
AB - 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.
KW - Odorant-binding proteins
KW - fluorescent proteins
KW - folding of proteins with beta-barrel topology
KW - protein stability
KW - small guanidine hydrochloride concentrations
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U2 - 10.1155/2010/935656
DO - 10.1155/2010/935656
M3 - Article
AN - SCOPUS:77954777045
SN - 0712-4813
VL - 24
SP - 367
EP - 373
JO - Spectroscopy
JF - Spectroscopy
IS - 3-4
ER -