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

Research output: Contribution to journalArticle

5 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 languageEnglish (US)
Pages (from-to)367-373
Number of pages7
JournalSpectroscopy
Volume24
Issue number3-4
DOIs
Publication statusPublished - Jul 26 2010

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Keywords

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

ASJC Scopus subject areas

  • Spectroscopy

Cite this

Stepanenko, O. V., Kuznetsova, I. M., Verkhusha, V. V., Staiano, M., D'Auria, S., & Turoverov, K. K. (2010). Denaturation of proteins with beta-barrel topology induced by guanidine hydrochloride. Spectroscopy, 24(3-4), 367-373. https://doi.org/10.3233/SPE-2010-0458