Role of secondary structure in protein-lipid interactions: decreases in the helical content of apolipoprotein C-I lower its affinity for triolein/water and phospholipid/triolein/water interfaces

被引：0

|

作者：

Meyers, Nathan ^{[1
]}

Wang, Libo ^{[1
]}

Gursky, Olga ^{[1
]}

Small, Donald ^{[1
]}

机构：

[1] Boston Univ, Boston, MA 02215 USA

来源：

FASEB JOURNAL | 2013年 / 27卷

关键词：

D O I：

暂无

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：

1208.9

引用

收藏

页数：1

相关论文

共 3 条

[1] Changes in helical content or net charge of apolipoprotein C-I alter its affinity for lipid/water interfaces
Meyers, Nathan L.
Wang, Libo
Gursky, Olga
Small, Donald M.
JOURNAL OF LIPID RESEARCH, 2013, 54 (07) : 1927 - 1938
[2] Apolipoprotein C-I Binds More Strongly to Phospholipid/Triolein/Water than Triolein/Water Interfaces: A Possible Model for Inhibiting Cholesterol Ester Transfer Protein Activity and Triacylglycerol-Rich Lipoprotein Uptake
Meyers, Nathan L.
Wang, Libo
Small, Donald M.
BIOCHEMISTRY, 2012, 51 (06) : 1238 - 1248
[3] Role of secondary structure in protein-phospholipid surface interactions:: Reconstitution and denaturation of apolipoprotein C-I:DMPC complexes
Benjwal, Sangeeta
Jayaraman, Shobini
Gursky, Olga
BIOCHEMISTRY, 2007, 46 (13) : 4184 - 4194