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

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-...

Full description

Saved in:
Bibliographic Details
Main Authors: Meyers, Nathan L., Wang, Libo, Gursky, Olga, Small, Donald M.
Format: Artigo
Language:Inglês
Published: The American Society for Biochemistry and Molecular Biology 2013
Subjects:
Research Articles
Online Access:https://ncbi.nlm.nih.gov/pmc/articles/PMC3679394/
https://ncbi.nlm.nih.gov/pubmed/23670531
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1194/jlr.M037531
Tags: Add Tag
No Tags, Be the first to tag this record!

Similar Items