RESUMO
In order to gain an insight into the mechanism of membrane insertion of the pore-forming protein colicin E(1) and the structure of its membrane-bound form, circular dichroism, fluorescence spectroscopy experiments were carried out. The results revealed the law of conformational changes by lipid membrane induction of the colicin E(1) molecule, and suggest that the lipid membranes with negative charges have a strong inducing action on colicin E(1) molecules. With the induction of membrane, the colicin E(1) molecules in different conformational states can all be recovered to the conformation of membrane insertion in native state. The induction intensity of different kinds of lipids on colicin E(1) was in the following order: DMPG>DMPE>DMPC. The binding of colicin E(1) with lipid vesicles was tight and the membrane-bound proteins were resistant to denaturation.
