This is an archive of papers published by the staff and faculty of Fox Chase Cancer Center. For questions about content, please contact Talbot Research Library
Last updated on
Rankin SE , Watts A , Roder H , Pinheiro TJT
Folding of apocytochrome c induced by the interaction with negatively charged lipid micelles proceeds via a collapsed intermediate state
Protein Science. 1999 Feb;8(2) :381-393
AbstractUnfolded apocytochrome c acquires an alpha-helical conformation upon interaction with lipid. Folding kinetic results below and above the lipid's CMC, together with energy transfer measurements of lipid bound states, and salt-induced compact states in solution, show that the folding transition of apocytochrome c from the unfolded state in solution to a lipid- inserted helical conformation proceeds via a collapsed intermediate state (I-C). This initial compact state is driven by a hydrophobic collapse of the polypeptide chain in the absence of the heme group and may represent a hems-free analogue of an early compact intermediate detected on the folding pathway of cytochrome c in solution. Insertion into the lipid phase occurs via an unfolding step of I-C through a more extended state associated with the membrane surface (I-S). While I-C appears to be as compact as salt-induced compact states in solution with substantial alpha-helix content, the final lipid-inserted state (H-mic) is as compact as the unfolded state in solution at pH 5 and has an alpha-helix content which resembles that of native cytochrome c.
NotesTimes Cited: 5 English Article 164VG PROTEIN SCI