A complete NMR spectral assignment of the lipid-free mouse apolipoprotein A-I (apoAI) C-terminal truncation mutant, apoAI(1-216)

• Published in: Biomolecular NMR assignments Vol. 1; no. 1; pp. 109 - 111
• Main Authors: Yang, Yunhuang, Hoyt, David, Wang, Jianjun
• Format: Journal Article
• Language: English
• Published: Netherlands Springer Nature B.V 01.07.2007
• Subjects: Animals; Apolipoprotein A-I - chemistry; Apolipoprotein A-I - genetics; Lipids; Lipids - chemistry; Low density lipoprotein; Mice; Molecular Structure; Nuclear Magnetic Resonance, Biomolecular; Peptide Fragments - chemistry; Peptide Fragments - genetics; Protein Structure, Secondary; Recombinant Proteins - chemistry; Recombinant Proteins - genetics; Sequence Deletion
• ISSN: 1874-2718; 1874-270X; 1874-270X
• DOI: 10.1007/s12104-007-9031-2

ApoAI is the major protein component of the high-density lipoprotein (HDL) that has been a hot subject of interests because of its anti-atherogenic properties. Lipid-free apoAI specifically binds to phospholipids, triggering HDL formation. Here we report a complete backbone assignment and nearly complete sidechain assignment of a C-terminal 24-residue truncation mutant of mouse apoAI, apoAI(1-216), in its lipid-free form.