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- W2102003454 endingPage "113" @default.
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- W2102003454 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." @default.
- W2102003454 created "2016-06-24" @default.
- W2102003454 creator A5059238682 @default.
- W2102003454 creator A5074212421 @default.
- W2102003454 date "2012-01-01" @default.
- W2102003454 modified "2023-09-25" @default.
- W2102003454 title "Mutual effects of disorder and order in fusion proteins between intrinsically disordered domains and fluorescent proteins" @default.
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- W2102003454 doi "https://doi.org/10.1039/c1mb05244f" @default.
- W2102003454 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21850362" @default.
- W2102003454 hasPublicationYear "2012" @default.
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