Title : Conformational flexibility of the N-terminal domain of apolipoprotein a-I bound to spherical lipid particles.

Pub. Date : 2008 Oct 28

PMID : 18831538






3 Functional Relationships(s)
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1 Taking advantage of a significant increase in fluorescence when a pyrene-labeled helix is in contact with the lipid surface, we monitored the behaviors of the N- and C-terminal helices upon binding of apoA-I to egg PC small unilamellar vesicles. pyrene apolipoprotein A1 Homo sapiens
2 Comparison of the binding isotherms for pyrene-labeled apoA-I as well as a C-terminal helical peptide suggests that an increase in surface concentration of apoA-I causes dissociation of the N-terminal helix from the surface leaving the C-terminal helix attached. pyrene apolipoprotein A1 Homo sapiens
3 Comparison of the binding isotherms for pyrene-labeled apoA-I as well as a C-terminal helical peptide suggests that an increase in surface concentration of apoA-I causes dissociation of the N-terminal helix from the surface leaving the C-terminal helix attached. pyrene apolipoprotein A1 Homo sapiens