Chemistry Reference
In-Depth Information
Fig. 7.4
A typical ground state configuration with energy of
34 of the 48mer in a 3D free space.
A hydrophobic central core is formed to maximize the number of H-H contacts. The
black and
gray beads
represent the polar and the hydrophobic residues, respectively, and the size of the beads
is merely for visualization purpose without correspondence to the real size of the residues. Graphic
is created by VMD [
52
]
−
103mer in 3D free space. A peak appears at
T
50 which signifies the transition
from an extended coil to a rather compact globular structure. A weak shoulder is
found at
T
≈
0
.
25 representing the rearrangements of bonds to bring the globule to
a even more compact state with a lower energy. As the magnitude of the surface field
increases, the folding process first becomes more complex, but when the surface
field is infinitely attractive so that the protein must lie entirely on the surface, only
a single specific heat peak is seen at
T
≈
0
.
38. This suggests that the transition
behavior is somewhat “simplified” into a single step process, where the adsorbed,
extended coil transforms into an absorbed, compact globular conformation.
≈
0
.
Fig. 7.5
Typical ground state configurations with energy of
21 of the 48mer attached to a surface
of infinite strength. This configuration has an intact hydrophobic core. The
black and gray beads
represent the polar and the hydrophobic residues, respectively, the
white beads
represent the sur-
face. The size of the beads is merely for visualization purpose without correspondence to the real
size of the residues. Graphic is created by VMD [
52
]
−
