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Issue 53, 2017
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Dissecting mechanism of coupled folding and binding of an intrinsically disordered protein by chemical synthesis of conformationally constrained analogues

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Abstract

Non-canonical α-methyl amino acids were incorporated at various sites in the sequence of intrinsically disordered activation domain from the p160 transcriptional co-activator (ACTR) to facilitate the formation of α-helical structures. Kinetic and thermodynamic data confirm the induced fit mechanism of complex formation between the synthesized ACTR variants and the nuclear co-activator binding domain (NCBD).

Graphical abstract: Dissecting mechanism of coupled folding and binding of an intrinsically disordered protein by chemical synthesis of conformationally constrained analogues

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Publication details

The article was received on 25 Mar 2017, accepted on 25 May 2017 and first published on 12 Jun 2017


Article type: Communication
DOI: 10.1039/C7CC02276J
Citation: Chem. Commun., 2017,53, 7369-7372
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    Dissecting mechanism of coupled folding and binding of an intrinsically disordered protein by chemical synthesis of conformationally constrained analogues

    B. Schmidtgall, O. Chaloin, V. Bauer, M. Sumyk, C. Birck and V. Torbeev, Chem. Commun., 2017, 53, 7369
    DOI: 10.1039/C7CC02276J

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