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Spectroscopy
Volume 24 (2010), Issue 3-4, Pages 367-373
http://dx.doi.org/10.3233/SPE-2010-0458

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

Olesya V. Stepanenko,1,4 Irina M. Kuznetsova,1 Vladislav V. Verkhusha,2 Maria Staiano,3 Sabato D'Auria,3 and Konstantin K. Turoverov1

1Institute of Cytology of the Russian Academy of Sciences, St. Petersburg, Russia
2Albert Einstein College of Medicine, New York, USA
3Institute of Protein Biochemistry CNR, Napoli, Italy
4Institute of Cytology of the Russian Academy of Sciences, Tikhoretsky av. 4, 194064 St. Petersburg, Russia

Copyright © 2010 Hindawi Publishing Corporation. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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.