Title : Fluorescence study of domain structure and lipid interaction of human apolipoproteins E3 and E4.

Pub. Date : 2014 Dec

PMID : 25281910






2 Functional Relationships(s)
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1 Upon binding of apoE3 and apoE4 variants to egg phosphatidylcholine small unilamellar vesicles, similar changes in Trp fluorescence or FRET efficiency were observed for the isoforms, indi- cating that the opening of the N-terminal helix bundle occurs similarly in apoE3 and apoE4. Phosphatidylcholines apolipoprotein E Homo sapiens
2 Upon binding of apoE3 and apoE4 variants to egg phosphatidylcholine small unilamellar vesicles, similar changes in Trp fluorescence or FRET efficiency were observed for the isoforms, indi- cating that the opening of the N-terminal helix bundle occurs similarly in apoE3 and apoE4. Phosphatidylcholines apolipoprotein E Homo sapiens