NMR studies of lipoprotein structure.
Early NMR structural studies of serum lipoproteins were based on (1)H, (13)C, (31)P, and (2)H studies of lipid components. From the early studies information on composition, lipid chain dynamics and order parameters, and monolayer organization resulted. More recently, selective or complete isotopic labeling techniques, combined with multidimensional NMR spectroscopy, have resulted in structural information of apoprotein fragments. Finally, use of heteronuclear three- and four-dimensional experiments have yielded solution structures and protein-lipid interactions of intact apolipoproteins C-I, C-II, and A-I.
Cushley
Robert J
RJ
Department of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby V5A 1S6, British Columbia, Canada. cushley@sfu.ca
Okon
Mark
M
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D001053:Apolipoproteins / Q000737:chemistry; D006801:Humans; D008055:Lipids / Q000737:chemistry*; D008074:Lipoproteins / Q000097:blood / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017434:Protein Structure, Tertiary
D001053:Apolipoproteins; D008055:Lipids; D008074:Lipoproteins