Conformational changes of a mitochondrial precursor protein on binding to phospholipid vesicles and SDS micelles. A circular dichroism and fluorescence spectroscopy study.
Conformations of an artificial mitochondrial precursor protein pCox IV-DHFR have been analyzed by CD and fluorescence spectroscopy in the presence of (cardiolipin-rich) phospholipid vesicles or SDS micelles. Binding of pCox IV-DHFR to phospholipid vesicles involves a conformational change, which is presequence-dependent, accompanies alteration in the secondary structure of the DHFR moiety, but is different from total unfolding of the polypeptide chain. On the other hand, a conformational change of the fusion protein on binding to the micelles of a positively charged detergent, SDS, is not presequence-dependent.
Endo
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Department of Chemistry, College of Technology, Gunma University, Kiryu, Japan.
Oya
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D002942:Circular Dichroism; D003102:Colloids; D004926:Escherichia coli / Q000378:metabolism; D008823:Micelles; D008928:Mitochondria / Q000378:metabolism*; D010743:Phospholipids / Q000378:metabolism*; D011487:Protein Conformation; D011498:Protein Precursors / Q000378:metabolism*; D012967:Sodium Dodecyl Sulfate; D013050:Spectrometry, Fluorescence
D003102:Colloids; D008823:Micelles; D010743:Phospholipids; D011498:Protein Precursors; D012967:Sodium Dodecyl Sulfate