Further study on the spontaneous partial folding of chicken heart apocytochrome c.
It has been previously reported (Biochem. Mol. Biol. Int., 30(5), 867-876, 1993) that chicken heart apocytochrome c has stronger tendency to fold spontaneously in aqueous solution than those from other species, and the relevance of its folding state with its ability to penetrate across the lipid bilayers has also been studied. In the present paper, the spontaneous folding characteristics of chicken heart apocytochrome c was further examined by the studies of Fourier-transform infrared spectra, the properties of intrinsic tryptophan fluorescence, and the measurements of hydrophobicity. In addition, it was also demonstrated that the partially-folded apocytochrome c is easily to be aggregated and hence relatively incompetent for translocation across the phospholipid bilayers.
Tong
J
J
National Laboratory of Biomacromolecules, Academia Sinica, Beijing, China.
Han
X
X
Yang
F
F
D000818:Animals; D001059:Apoproteins / Q000737:chemistry*; D002645:Chickens; D003574:Cytochrome c Group / Q000737:chemistry*; D045304:Cytochromes c; D005454:Fluorescence Polarization; D009206:Myocardium / Q000737:chemistry*; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017550:Spectroscopy, Fourier Transform Infrared; D013499:Surface Properties; D014364:Tryptophan / Q000737:chemistry
D001059:Apoproteins; D003574:Cytochrome c Group; D014364:Tryptophan; D045304:Cytochromes c