Figure 2.
Figure 2 Membrane insertion and orientation of endophilin
N-terminal amphipathic helix. (A) Oxygen (red circles) and
NiEDDA (green squares) accessibilities ( )
of membrane-bound N-BAR domain as a function of label position.
The graph below shows a ln( ratio)
plot ( )
showing the differential access of colliders to the spin label
and the penetration of hydrophobic residues into the membrane.
The periodic oscillation is indicative of a helical structure.
Equivalent maxima indicate that the helix lies planar to the
membrane. (B) Helical wheel representation showing hydrophobic
and charged faces. (C) Model of the amphipathic helix, residues
1–16 with hydrophobic residues coloured green and surface
charge potential also shown. (D) Model of the N-BAR amphipathic
helix to scale with PtdIns(4,5)P[2] and PtdSer lipids showing
the depth of penetration of the helix as calculated from data in
(A) and penetration measurements, described in Materials and
methods.
The above figure is reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
EMBO J
(2006,
25,
2898-2910)
copyright 2006.
)
of membrane-bound N-BAR domain as a function of label position.
The graph below shows a ln( 
)
showing the differential access of colliders to the spin label
and the penetration of hydrophobic residues into the membrane.
The periodic oscillation is indicative of a helical structure.
Equivalent maxima indicate that the helix lies planar to the
membrane. (B) Helical wheel representation showing hydrophobic
and charged faces. (C) Model of the amphipathic helix, residues
1–16 with hydrophobic residues coloured green and surface
charge potential also shown. (D) Model of the N-BAR amphipathic
helix to scale with PtdIns(4,5)P[2] and PtdSer lipids showing
the depth of penetration of the helix as calculated from data in
(A) and penetration measurements, described in Materials and
methods.