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A
B
Pleat Surface
B
C
T e rmini Surface
Lamination
D
E
T e rmini Surface
Figure 1.10
(
A
) Fiber-pleat (
B
) and -termini (
C
) surfaces vs. tube termini
β
(
-sheet lamination in
the tube hides the pleat surface, exposing only the termini
surface which is composed of only the side chains at the
peptide termini and displays the laminate grooves. The anti-
parallel
D, E
) surface of KLVFFAE. Extended
β
-sheets results in both N and C terminal residues
being displayed at the termini surfaces, resulting in the blue
(lysine) and red (glutamic acid) alternating pattern (
)
for the fibers. The tubes which are also anti-parallel, but
out-of-register
A-C
β
-sheets, result in prominently displayed
β
lysines (
-sheets (not shown) would have
unique termini surfaces composed of the N and C terminal
side chains, respectively. The protonation of the charged
glutamic acid in KLVFFAE nanotubes or mutation to non-
charged leucine (KLVFFAL), results in distinct surface charge
modulation. This charge enables binding of negatively charge
Au nanoparticles [106].
D, E
). Parallel
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