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Table 2 The secondary structure and orientation of helix, beta sheet and lipid acyl chain of FP, TMD and FP/TMD 1:1 complex in DMPC:DMPG 1:1 vesicular solution with L/P = 50 at pH 5.0. Values were obtained by averaging three or four sets of data.

From: Membrane interaction and structure of the transmembrane domain of influenza hemagglutinin and its fusion peptide complex

  Lipid FP TMD Complex
Secondary structure     
   α-helix (%)   26 ± 3 64 ± 1 46 ± 7
   β-sheet (%)   55 ± 5 20 ± 2 28 ± 1
   Unordered (%)   9 ± 3 --- 9 ± 8
   β-turns (%)   11 ± 3 17 ± 4 17 ± 3
Helix axis orientation     
    R ATR   1.82 ± 0.01 2.46 ± 0.22 2.07 ± 0.08
   Θ (°)   60 ± 1 34 ± 1 49 ± 2
Beta-strand orientation     
    R ATR   1.18 ± 0.10 N.A. 1.28 ± 0.20
   Φ (°)   56 ± 5 N.A. 52 ± 7
Acyl chain tilt angle     
    R ATR 1.09 ± 0.09 1.78 ± 0.45 1.31 ± 0.04 1.62 ± 0.12
   δ (°) 27 ± 4 49 ± 12 36 ± 1 45 ± 4