Issue 1, 2012
From the journal:

Molecular BioSystems

Mutual effects of disorder and order in fusion proteins between intrinsically disordered domains and fluorescent proteins†

Marina Lotti*a  and  Sonia Longhi*b  

* Corresponding authors

a Dipartimento di Biotecnologie e Bioscienze, Università Statale Milano-Bicocca, Piazza della Scienza 2, 20126 Milan, Italy
E-mail: marina.lotti@unimib.it
Fax: +39 02 64 48 35 69
Tel: +39 02 64 48 35 27

b Architecture et Fonction des Macromolécules Biologiques, UMR 6098 CNRS et Universités d'Aix-Marseille I et II, Avenue de Luminy, 163, Case 932, 13288 Marseille Cedex 09, France
E-mail: Sonia.Longhi@afmb.univ-mrs.fr
Fax: +33 4 91 26 67 20
Tel: +33 4 91 82 55 80

Abstract

Intrinsically disordered proteins are being paid an increasing amount of interest due to the understanding of the crucial role that flexible regions play in molecular recognition and in signaling. Accordingly, reports focusing on the structural and functional characterization of intrinsically disordered proteins or regions are growing exponentially. Relatively few studies have however been reported on the mutual effects of ordered and disordered moieties in artificial fusion proteins. In this review, we focus on the few available experimental data based on the use of chimeras in which fluorescent proteins were fused to disordered domains of different lengths, compactness and propensity to form secondary structures. The impact of the artificial fusion on the conformational and functional properties of the resulting proteins is discussed.

Graphical abstract: Mutual effects of disorder and order in fusion proteins between intrinsically disordered domains and fluorescent proteins

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Article information

DOI
https://doi.org/10.1039/C1MB05244F
Article type
Review Article
Submitted
17 Jun 2011
Accepted
27 Jul 2011
First published
18 Aug 2011

Mol. BioSyst., 2012,8, 105-113

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Mutual effects of disorder and order in fusion proteins between intrinsically disordered domains and fluorescent proteins

M. Lotti and S. Longhi, Mol. BioSyst., 2012, 8, 105 DOI: 10.1039/C1MB05244F

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