Dissecting mechanism of coupled folding and binding of an intrinsically disordered protein by chemical synthesis of conformationally constrained analogues - Archive ouverte HAL
Journal Articles Chemical Communications Year : 2017

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

Abstract

Non-canonical alpha-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 alpha-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).
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hal-03676439 , version 1 (23-05-2022)

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Boris Schmidtgall, Olivier Chaloin, Valentin Bauer, Manuela Sumyk, Catherine Birck, et al.. Dissecting mechanism of coupled folding and binding of an intrinsically disordered protein by chemical synthesis of conformationally constrained analogues. Chemical Communications, 2017, 53 (53), pp.7369-7372. ⟨10.1039/c7cc02276j⟩. ⟨hal-03676439⟩
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