Correlation between unfolded states of apocytochrome c and its ability to pass lipid bilayer.
In contrast to the horse heart apocytochrome c, the chicken heart apocytochrome c underwent a conformational change from random coil to partial folding during a renaturation process. When the apocytochrome horse heart and that of chicken heart c were subjected to a translocation assay in vitro using large trypsin-enclosed unilamellar vesicles from soybean phospholipids, the ability of the chicken heart apocytochrome c to penetrate into the liposomes was found to decrease markedly with the renaturation procedure, while that of horse heart apocytochrome c remained relatively constant. Observations from circular dichroism measurement on the induction of secondary folding of these two species of apocytochrome c upon interaction with soybean phospholipid vesicles suggested that a more flexible structure of apocytochrome c embedded in the lipid matrix be required for its efficient translocation across the bilayer.
Wang
X S
XS
National Laboratory of Biomacromolecules, Institute of Biophysics, Academia Sinica, Beijing, PRC.
Tong
J C
JC
Han
X H
XH
Yang
F Y
FY
D000595:Amino Acid Sequence; D000818:Animals; D001059:Apoproteins / Q000737:chemistry* / Q000235:genetics; D002645:Chickens; D003574:Cytochrome c Group / Q000737:chemistry* / Q000235:genetics; D045304:Cytochromes c; D006736:Horses; D008051:Lipid Bilayers; D008969:Molecular Sequence Data; D009695:Nucleic Acid Renaturation; D010743:Phospholipids; D017510:Protein Folding
D001059:Apoproteins; D003574:Cytochrome c Group; D008051:Lipid Bilayers; D010743:Phospholipids; D045304:Cytochromes c