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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