One such circumstance could have been the need for a binding mechanism, as presented in [6], which posits a compositionality model where synfire chain waves [7] represent semantic atoms and synchronization of activity in different chains serves as a binding mechanism.
Because of the one-residue stagger between chains, equivalent residues in different chains of a collagen homotrimer have non-equivalent chemical environments.
The basic idea is to improve the running time by assigning fragments to clusters that can be chained separately from each other without resulting in different chaining outcome.
Consistent with this observation, for the reported influenza A/H3N2 virus HA2 structure (PDB entry 1QU1) where there are two trimers in the asymmetric unit, this region displays different conformations, including α-helix, β-sheet, or random coil, in different chains.
Above this temperature, part of the lipids are still ordered and probably form a type of complex with B12, in which the chains are in a different chain lattice.
After burn-in, the different chains oscillate around the same mean with similar variances, despite differences in starting point.
Due to the crowdedness effect of the crystal lattice, residues Arg, Thr, Pro, Gly, Cys, Glu, and Ala in a different chain (chain B) directly interact with the covalent-orlistat in the current chain (chain A).
In addition, the different chain structures of the two groups result in different cleavage angles.
