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

Issue title: From Molecule to Tissue: XIII European Conference on the Spectroscopy of Biological Molecules, Palermo, Italy, August 28–September 2, 2009, Part 2 of 2

Article type: Research Article

Authors: Stepanenko, Olesya V.^; | Kuznetsova, Irina M. | Verkhusha, Vladislav V. | Staiano, Maria | D'Auria, Sabato | Turoverov, Konstantin K.

Affiliations: Institute of Cytology of the Russian Academy of Sciences, St. Petersburg, Russia | Albert Einstein College of Medicine, New York, USA | Institute of Protein Biochemistry CNR, Napoli, Italy

Note: [] Corresponding author: Dr. Olesya V. Stepanenko, Institute of Cytology of the Russian Academy of Sciences, Tikhoretsky av. 4, 194064 St. Petersburg, Russia. Tel.: +7 812 247 19 57; Fax: +7 812 247 03 41; E-mail: lvs@mail.cytspb.rssi.ru.

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

DOI: 10.3233/SPE-2010-0458

Journal: Spectroscopy, vol. 24, no. 3-4, pp. 367-373, 2010