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Chem Commun (Camb). 2017 Jun 29;53(53):7369-7372. doi: 10.1039/c7cc02276j.

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

Author information

1
ISIS (Institut de Science et d'Ingénierie Supramoléculaires) & icFRC (International Center for Frontier Research in Chemistry), University of Strasbourg and CNRS - UMR 7006, Strasbourg, France. torbeev@unistra.fr.

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).

PMID:
28604862
DOI:
10.1039/c7cc02276j
[Indexed for MEDLINE]

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