NMR structure of human apolipoprotein C-II in the presence of sodium dodecyl sulfate

Christopher A. MacRaild, Danny M. Hatters, Geoffrey J. Howlett, Paul R. Gooley

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64 Citations (Scopus)


The structure and protein-detergent interactions of apolipoprotein C-II (apoC-II) in the presence of SDS micelles have been investigated using circular dichroism and heteronuclear NMR techniques applied to 15N-labeled protein. Micellar SDS, a commonly used mimetic of the lipoprotein surface, inhibits the aggregation of apoC-II and induces a stable structure containing approximately 60% α-helix as determined by circular dichroism. NMR reveals the first 12 residues of apoC-II to be structurally heterogeneous and largely disordered, with the rest of the protein forming a predominantly helical structure. Three regions of helical conformation, residues 16-36, 50-56, and 63-77, are well-defined by NMR-derived constraints, with the intervening regions showing more loosely defined helical conformation. The structure of apoC-II is compared to that determined for other apolipoproteins in a similar environment. Our results shed light on the lipid interactions of apoC-II and its mechanism of lipoprotein lipase activation.

Original languageEnglish
Pages (from-to)5414-5421
Number of pages8
Issue number18
Publication statusPublished - 8 May 2001
Externally publishedYes

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