4 research outputs found
Synthetic β‑Barrel by Metal-Induced Folding and Assembly
The
de novo construction of repeat proteins has received much attention
from biologists and chemists, yet that of a β-barrel structure,
one of the most well-known classes, has not been accomplished to date.
Here, we report the first chemical construction of a β-barrel
tertiary structure with a pore through a combination of peptide folding
and metal-directed self-assembly. Coordination of zinc salts to an
eight-residue peptide fragment bearing β-strand- and loop-forming
sequences resulted in a β-barrel in which six-stranded cylindrical
antiparallel β-sheets formed a hydrophobic pore with a specific
shape
Synthetic β‑Barrel by Metal-Induced Folding and Assembly
The
de novo construction of repeat proteins has received much attention
from biologists and chemists, yet that of a β-barrel structure,
one of the most well-known classes, has not been accomplished to date.
Here, we report the first chemical construction of a β-barrel
tertiary structure with a pore through a combination of peptide folding
and metal-directed self-assembly. Coordination of zinc salts to an
eight-residue peptide fragment bearing β-strand- and loop-forming
sequences resulted in a β-barrel in which six-stranded cylindrical
antiparallel β-sheets formed a hydrophobic pore with a specific
shape
Mutual Induced Fit in a Synthetic Host–Guest System
Mutual
induced fit is an important phenomenon in biological molecular
recognition, but it is still rare in artificial systems. Here we report
an artificial host–guest system in which a flexible calix[4]Âarene
is enclathrated in a dynamic self-assembled host and both molecules
mutually adopt specific three-dimensional structures. NMR data revealed
the conformational changes, and crystallographic studies clearly established
the precise structures at each stage
Synthetic β‑Barrel by Metal-Induced Folding and Assembly
The
de novo construction of repeat proteins has received much attention
from biologists and chemists, yet that of a β-barrel structure,
one of the most well-known classes, has not been accomplished to date.
Here, we report the first chemical construction of a β-barrel
tertiary structure with a pore through a combination of peptide folding
and metal-directed self-assembly. Coordination of zinc salts to an
eight-residue peptide fragment bearing β-strand- and loop-forming
sequences resulted in a β-barrel in which six-stranded cylindrical
antiparallel β-sheets formed a hydrophobic pore with a specific
shape