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Updated: Aug 18, 2026

Examining the Conformational Dynamics of Membrane Proteins in situ with Site-directed Fluorescence Labeling
Published on: May 29, 2011
Studies on the Conformation of Apocytochrome c in Different Folding States Inserted into the Membranes
Xue-Hai Han1, Sen-Fang Sui, Fu-Yu Yang
1National Laboratory of Biomacromolecules, Institute of Biophysics Academia Sinica, Beijing 100101, China.
Abstract:
Correlation between the folding states of the chicken heart apocytochrome c and its membrane insertion ability was studied by the monolayer experiment. The penetration ability of apocytochrome c decreased with its folding. Intrinsic fluorescence emissions of apocytochrome c interacted with soybean phospholipids liposomes suggested that the conformations of apocytochrome c with different folding states in aqueous solution were also different in the membranes. The conformational differences were further characterized by CD spectra of apocytochrome c interacted with DMPC and DMPG liposomes. The results showed that apocytochrome c, which were randomly coiled in aqueous solution, adopted alpha-helical conformations after interaction with DMPG liposome. The apocytochrome c with a folded state in aqueous solution also adopted alpha-helical conformations, but the alpha-helical contents were less than the former. When DMPC liposomes were used, no distinct conformational change was observed.
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