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NMR Structural Studies of a 180 kDa HDL Particle

EMSL Project ID


This research proposal centers on exploring NMR study of a 180 kDa HDL particle.
In particular, we will concentrate on the NMR study of discoidal HDL particle, which is the initial stage of HDL during mature HDL assebly. The discoidal HDL activate an enzyme, LCAT, that convert "bad cholesterol" into cholesterol ester. The newly produced cholesterol ester will be loaded into discoidal HDL, resulting in maturation of HDL for transport of the "bad cholesterol" back to the liver for clearance. Our recent data suggests that we can prepare reconstituted discoidal HDL particle for NMR study. We developed a method to further purify this discoidal HDL and prepared a NMR sample. Our preliminary NMR data on a 500 MHz NMR machine is really promising. We suggest that the NMR technique is the optimal technique in this case, since HDL particles resist forming crystals. Thus, we request high-field NMR time, such as 750/800/900 MHz NMR time for this project. This is the first structural study of a HDL particle.

Project Details

Project type
Capability Research
Start Date
End Date


Principal Investigator

Jianjun Wang
Wayne State University

Team Members

Yonghong Zhang
Wayne State University

Arun Sivashanmugam
Wayne State University

Jianglei Chen
Wayne State University

Bin Chen
Wayne State University

Related Publications

A complete backbone spectral assignment of human apolipoprotein AI on a 38 kDa preβHDL (Lp1-AI) particle Xuefeng Ren, Yunhuang Yang, Tracey Neville, David Hoyt, Daniel Sparks, Jianjun Wang
Chen B, X Ren, T Neville, WG Jerome, DW Hoyt, DL Sparks, G Ren, and J Wang. 2009. "Apolipoprotein AI tertiary structures determine stability and phospholipid-binding activity of discoidal high-density lipoprotein particles of different sizes." Protein Science 18(5):921-935. doi:10.1002/pro.101