Ligand escape pathways and (un)binding free energy calculations for the hexameric insulin-phenol complex.

@article{Vashisth2008LigandEP,
  title={Ligand escape pathways and (un)binding free energy calculations for the hexameric insulin-phenol complex.},
  author={Harish Vashisth and Cameron F. Abrams},
  journal={Biophysical journal},
  year={2008},
  volume={95 9},
  pages={4193-204}
}
Cooperative binding of phenolic species to insulin hexamers is known to stabilize pharmaceutical preparations of the hormone. Phenol dissociation is rapid on hexamer dissolution timescales, and phenol unbinding upon dilution is likely the first step in the conversion of (pharmaceutical) hexameric insulin to the active monomeric form upon injection. However, a clear understanding of the determinants of the rates of phenol unbinding remains obscure, chiefly because residues implicated in phenol… CONTINUE READING

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