Issue 53, 2017

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

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

Supplementary files

Article information

Article type
Communication
Submitted
25 Marts 2017
Accepted
25 Maijs 2017
First published
12 Jūn. 2017

Chem. Commun., 2017,53, 7369-7372

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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