Changes in helical content or net charge of apolipoprotein C-I alter its affinity for lipid/water interfaces[S]

Amphipathic α-helices mediate binding of exchangeable apolipoproteins to lipoproteins. To probe the role of α-helical structure in protein-lipid interactions, we used oil-drop tensiometry to characterize the interfacial behavior of apolipoprotein C-I (apoC-I) variants at triolein/water (TO/W) and 1-...

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Bibliographic Details
Main Authors: Nathan L. Meyers, Libo Wang, Olga Gursky, Donald M. Small
Format: Article
Language:English
Published: Elsevier 2013-07-01
Series:Journal of Lipid Research
Subjects:
Online Access:http://www.sciencedirect.com/science/article/pii/S0022227520421406