Biomedical Engineering Reference
In-Depth Information
OR
OR
OR
RO
RO
O
O
O
RO
RO
RO
RO
RO
RO
RO
OCH
3
OCH
3
OCH
3
R = peptides attached though linker regions
P
e
p
t
i
d
e
P
e
p
t
i
d
e
P
e
p
t
i
d
e
P
e
p
t
i
d
e
P
e
p
t
i
d
e
NH
HN
HN
NH
P
e
p
t
i
d
e
N
N
O
O
O
O
O
O
O
NH
O
O
O
O
O
O
O
OCH
3
HN
O
SS
D
-Gal
p
template
cyclo
-DTT template
Figure 6.8 Schematic presentation of carboproteins
carboprotein monomers, as the 2
2-helix structure adopted a more
compact conformation. Furthermore, the clear conformational differ-
ences observed between the two 4-helix (3
þ
1) carboproteins based on
D
-altropyranoside and
D
-galactopyranoside supports the notion that
the folding is affected by the template and that subtle variations in
template distance-geometry design may be exploited to template-
control the solution fold.
In an application to nanobioscience, a hemi-4-helix bundle designed
to dimerize was synthesized by attaching two copies of an a-helical
peptide to a cyclo-DTT template [146]. This hemi-4-helix bundle
formed a SAM on Au(111) with 2
2-helix bundle formation, providing
4-helix bundle diameters of 23-27
˚
. Both parallel and antiparallel 2
2-
helix bundles were believed to be formed, with the latter providing better
electron tunneling due to compensation of the dipole moment of the two
halves.
Search WWH ::
Custom Search