Electrostatic and hydrophobic contributions to the folding mechanism of apocytochrome c driven by the interaction with lipid.

@article{Rankin1998ElectrostaticAH,
  title={Electrostatic and hydrophobic contributions to the folding mechanism of apocytochrome c driven by the interaction with lipid.},
  author={Stephen E Rankin and Anthony Watts and Teresa T. J. Pinheiro},
  journal={Biochemistry},
  year={1998},
  volume={37 36},
  pages={12588-95}
}
In aqueous solution, while cytochrome c is a stably folded protein with a tightly packed structure at the secondary and tertiary levels, its heme-free precursor, apocytochrome c, shows all features of a structureless random coil. However, upon interaction with phospholipid vesicles or lysophospholipid micelles, apocytochrome c undergoes a conformational transition from its random coil in solution to an alpha-helical structure on association with lipid. The driving forces of this lipid-induced… CONTINUE READING

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