Heteronuclear NMR studies of human serum apolipoprotein A‐I

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Abstract
The apolipoprotein A‐I (apoA‐I) solution structure in the presence of sodium dodecyl sulfate (SDS) was determined by combination of chemical shift index and torsion angle likelihood obtained from shift and sequence similarity methods. ApoA‐I in lipid‐mimetic solution is composed of α‐helices (residues 8–32, 45–64, 67–77, 82–86, 90–97, 100–118, 122–140, 146–162, 167–205, 210–216 and 221–239), with 2–5 residue irregular segments between helical repeats, and the irregular segment 78–81 within helical repeat 2. ApoA‐I is a monomer in the SDS complex and no evidence of interhelical interactions is found. Comparison of the apoA‐I and apoA‐I(1–186) [Okon et al., FEBS Lett. 487 (2001) 390–396] solution structures revealed that apoA‐I undergoes a conformational change around Pro121.