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

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


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).

MeSH terms

  • Amino Acids / chemistry
  • Intrinsically Disordered Proteins / chemical synthesis*
  • Intrinsically Disordered Proteins / chemistry*
  • Kinetics
  • Protein Binding
  • Protein Conformation
  • Protein Folding*
  • Thermodynamics
  • Transcription Factors / chemistry


  • Amino Acids
  • Intrinsically Disordered Proteins
  • Transcription Factors