NMR studies of lipoprotein structure

被引:38
作者
Cushley, RJ [1 ]
Okon, M [1 ]
机构
[1] Simon Fraser Univ, Dept Mol Biol & Biochem, Burnaby, BC V5A 1S6, Canada
来源
ANNUAL REVIEW OF BIOPHYSICS AND BIOMOLECULAR STRUCTURE | 2002年 / 31卷
关键词
protein structure; apolipoproteins; conformation; heteronuclear; 3D;
D O I
10.1146/annurev.biophys.31.101101.140910
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Early NMR structural studies of serum lipoproteins were based on H-1, C-13, P-31, and H-1 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.
引用
收藏
页码:177 / 206
页数:32
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