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

Pub. Date : 2001 May 8

PMID : 11331005






4 Functional Relationships(s)
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1 NMR structure of human apolipoprotein C-II in the presence of sodium dodecyl sulfate. Sodium Dodecyl Sulfate apolipoprotein C2 Homo sapiens
2 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 (15)N-labeled protein. Sodium Dodecyl Sulfate apolipoprotein C2 Homo sapiens
3 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 (15)N-labeled protein. Sodium Dodecyl Sulfate apolipoprotein C2 Homo sapiens
4 Micellar SDS, a commonly used mimetic of the lipoprotein surface, inhibits the aggregation of apoC-II and induces a stable structure containing approximately 60% alpha-helix as determined by circular dichroism. Sodium Dodecyl Sulfate apolipoprotein C2 Homo sapiens