|
Figure 3.
FIGURE 3. A, stereo view of the backbone superposition of
the 100 Leu^23,Ala^24-sCT periodically sampled structures along
the 1000-ps unrestrained MD. Structures were superimposed for
pairwise minimum r.m.s. deviation of the N, C  , and C
atoms of residues 4–28. B, stereo view of Leu^23,Ala^24-sCT
structure showing the amphipathic property of the -helix;
hydrophobic residues, mainly leucine, are on the left side,
whereas hydrophilic amino acids are on the right side. Hydrogen
bonds along the backbone and in the N and C terminus helix cap
motifs are represented as discontinuous lines.
|
