Many one-dimensional (1D) nanostructures are constructed by self-assembly of peptides or peptide conjugates containing a short β-sheet sequence as the core building motif essential for the intermolecular hydrogen bonding that promotes directional, anisotropic growth of the resultant assemblies.
One noteworthy difference between human STIM-1 and -2, and other EF-hand domain sequences is the proposed β-sheet sequence (Fig. 4A) [33], [33].
The rc peptide was designed to be an unstructured random coil to provide a negative control; it is a randomly scrambled version of the β-sheet sequence, β.
This domain is followed by a proline-rich sequence, called the P-domain that folds into a long hairpin-like structure with two pairs of short anti-parallel β-sheet sequences.
Peptides containing alternating D- and L-amino acids have previously been shown to form extended structures (De Santis et al., 1974; Heitz et al., 1981), and they populate similar conformational space as our MD-identified α-sheet sequences consisting solely of L-amino acids.
Based on this, Kawahata et al. ( 2001) estimated that the maximum volume of high-temperature hydrothermal fluid is twice that of the upper oceanic crust (the volcanic and sheeted dike sequence) and if 65%to85%5% of the rocks are altered to secondary minerals, the volumetric water/rock ratio would be 2.3 to 3.1.
Figure 1a shows the synthesized peptide MASP1, comprising three structural units: a β-sheet forming sequence plus three glutamic acid residues, an oligoproline segment, and a hydrophobic hydrocarbon.
The peptide moiety GNNQQNY is a key β-sheet forming sequence derived from the yeast prion Sup35 and was chosen to afford the capacity for intermolecular hydrogen bonding between the designed DAs.
Peptides with β-sheet forming sequences derived from, or inspired by, amyloid proteins, have been extensively incorporated into various molecular building units to construct self-assembling one-dimensional (1D) nanostructures.
The α-helices and β-sheets have high sequence homology with variations in either absent β-sheets and loops or additional α-helices.
Their sequences and kinetic parameters were provided in Additional file 1 (sheet 1, mutant sequences and summary).
