Structural perturbation of super-folder GFP in the presence of guanidine thiocyanate

Olesya V. Stepanenko, Olga V. Stepanenko, Irina M. Kuznetsova, Vladislav V. Verkhusha, Konstantin K. Turoverov

Research output: Chapter in Book/Report/Conference proceedingChapter


The guanidine thiocyanate induced denaturation-renaturation of sfGFP was studied. It was shown that the disruption of sfGFP native structure occurs in the range of guanidine thiocyanate concentrations from 0.5 to 2.5 M. This process was accompanied by simultaneous changes of all recorded parameters. It was found that the small guanidine thiocyanate concentrations (less then 0.1-0.2 M) triggered local structural disturbances in protein which result in significant decrease of chromophore and tryptophan fluorescence intensity and change of protein visible absorption spectrum.

Original languageEnglish (US)
Title of host publicationSpectroscopy of Biological Molecules. Proceedings from the 14th European Conference on the Spectroscopy of Biological Molecules 2011
EditorsMaria Marques, Luis Batista de Carvalho, Parvez Haris
Number of pages6
StatePublished - Nov 27 2013

Publication series

NameAdvances in Biomedical Spectroscopy
ISSN (Print)1875-0656


  • Fluorescent proteins
  • folding of proteins with beta-barrel topology
  • small guanidine thiocyanate concentrations
  • super-folder GFP

ASJC Scopus subject areas

  • Radiology Nuclear Medicine and imaging


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