Journal of Spectroscopy

Journal of Spectroscopy / 2010 / Article
Special Issue

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

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Volume 24 |Article ID 935656 |

Olesya V. Stepanenko, Irina M. Kuznetsova, Vladislav V. Verkhusha, Maria Staiano, Sabato D'Auria, Konstantin K. Turoverov, "Denaturation of proteins with beta-barrel topology induced by guanidine hydrochloride", Journal of Spectroscopy, vol. 24, Article ID 935656, 7 pages, 2010.

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


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.

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.

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