@inbook{cc3a3482929847d0a0d425533452bcd3,
title = "Beta-Barrel Scaffold of Fluorescent Proteins. Folding, Stability and Role in Chromophore Formation.",
abstract = "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.",
keywords = "Chromophore and protein interaction, Fluorescence proteins, Hysteresis, Protein folding, RFP, Split GFP, Superfolder GFP, β-barrel scaffold",
author = "Stepanenko, {Olesya V.} and Stepanenko, {Olga V.} and Kuznetsova, {Irina M.} and Verkhusha, {Vladislav V.} and Turoverov, {Konstantin K.}",
note = "Funding Information: Our work reviewed in this chapter was supported by the Russian Federation MCB RAS and RFBP 12-04-31469-mol-a grants to K.K.T. and by the grants GM073913 and CA164468 from the US National Institutes of Health to V.V.V.",
year = "2013",
doi = "10.1016/B978-0-12-407699-0.00004-2",
language = "English (US)",
series = "International Review of Cell and Molecular Biology",
publisher = "Elsevier Inc.",
pages = "221--278",
booktitle = "International Review of Cell and Molecular Biology",
}