Beta-Barrel Scaffold of Fluorescent Proteins. Folding, Stability and Role in Chromophore Formation.

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

Research output: Chapter in Book/Report/Conference proceedingChapter

74 Scopus citations


This review focuses on the current view of the interaction between the β-barrel scaffold of fluorescent proteins and their unique chromophore located in the internal helix. The chromophore originates from the polypeptide chain and its properties are. influenced by the surrounding protein matrix of the β-barrel. On the other hand, it appears that a chromophore tightens the β-barrel scaffold and plays a crucial role in its stability. Furthermore, the presence of a mature chromophore causes hysteresis of protein unfolding and refolding. We survey studies measuring protein unfolding and refolding using traditional methods as well as new approaches, such as mechanical unfolding and reassembly of truncated fluorescent proteins. We also analyze models of fluorescent protein unfolding and refolding obtained through different approaches, and compare the results of protein folding in vitro to co-translational folding of a newly synthesized polypeptide chain.

Original languageEnglish (US)
Title of host publicationInternational Review of Cell and Molecular Biology
PublisherElsevier Inc.
Number of pages58
StatePublished - 2013

Publication series

NameInternational Review of Cell and Molecular Biology
ISSN (Print)1937-6448


  • Chromophore and protein interaction
  • Fluorescence proteins
  • Hysteresis
  • Protein folding
  • RFP
  • Split GFP
  • Superfolder GFP
  • β-barrel scaffold

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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