Denaturation of proteins with beta-barrel topology induced by guanidine hydrochloride

Olesya V. Stepanenko; Irina M. Kuznetsova; Vladislav V. Verkhusha; Maria Staiano; Sabato D'Auria; Konstantin K. Turoverov

doi:10.3233/SPE-2010-0458

Denaturation of proteins with beta-barrel topology induced by guanidine hydrochloride

Olesya V. Stepanenko, Irina M. Kuznetsova, Vladislav V. Verkhusha, Maria Staiano, Sabato D'Auria, Konstantin K. Turoverov

Anatomy & Structural Biology

Research output: Contribution to journal › Article › peer-review

6 Scopus citations

Abstract

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.

Original language	English (US)
Pages (from-to)	367-373
Number of pages	7
Journal	Spectroscopy
Volume	24
Issue number	3-4
DOIs	https://doi.org/10.3233/SPE-2010-0458
State	Published - Jul 26 2010

Keywords

Odorant-binding proteins
fluorescent proteins
folding of proteins with beta-barrel topology
protein stability
small guanidine hydrochloride concentrations

ASJC Scopus subject areas

Spectroscopy

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10.3233/SPE-2010-0458

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title = "Denaturation of proteins with beta-barrel topology induced by guanidine hydrochloride",

abstract = "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.",

keywords = "Odorant-binding proteins, fluorescent proteins, folding of proteins with beta-barrel topology, protein stability, small guanidine hydrochloride concentrations",

author = "Stepanenko, {Olesya V.} and Kuznetsova, {Irina M.} and Verkhusha, {Vladislav V.} and Maria Staiano and Sabato D'Auria and Turoverov, {Konstantin K.}",

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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 - 2010/7/26

Y1 - 2010/7/26

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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Denaturation of proteins with beta-barrel topology induced by guanidine hydrochloride

Abstract

Keywords

ASJC Scopus subject areas

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