Snap connectors
Contents
Crystolecules
Even very small crystolecule clips already have such high activation energies that
random thermal fluctuations do not accidentally open them up anymore.
Even if there a many mols worth of such snap connectors present and observed over a very long time.
(TODO: redo the math and add it here)
So usage of shape locking chains to guard against accidental thermal opening is most likely not necessary.
Holding chains together by clips or only VdW force can fully suffice.
Nanoscale clips could be designed such that they allow energy recuperation.
Same for VdW suck-in.
Foldamers (e.g. de-novo proteins)
Snap-together by mere touching
Energetic snap-together by shape complementarity hydrogen bonding and VdW forces is natural and obviously worth to go for.
See Van der Waals force sticking and VdW suck-in.
Clipping
The idea is to clip foldamers together using larger scale elastic deformation.
Te result would be is a form closure connection that may or may nor be energetically and/or structurally reversible re-openable.
Questionable benefits
Such a connection might have slightly higher mechanical stability than a mare surface contact snap-together.
But likely not by much, since internal cohesion of proteins is also not providing dense a polycyclic covalent network.
Unless the protein backbone has been heavily covalently cross-linked, which is difficult.
Potential challenges
Clips need active force applying actuation. That means:
- thermally driven selfassembly is no longer an option (a huge loss) and
- some form of positional assembly is needed. Either bottom up positional assembly or top down positional assembly
For proteins to reach around parts of other proteins (like a clamp) such that they are not only shape complementary but also can do large scale deformation clipping actions, they need to be quite large (quite far into tertiary structure). This may make de-novo protein engineering harder.
Alternatives to reach higher bonding strengths between de-novo proteins include:
- covalent cross-linking after quaternary assembly
Related to de-novo protein clipping
The folded-foldamer pushing approach.
Empolying extensive form closure assembly and rebar-style-tensionsing not only in advaned gemstone based nanosystems but already in earlier foldamer based nanosystems.
This likely is not sensible is seems due to proteins being to soft rough and sticky.
Even de-novo proteins specifically enginnered to be stiff and of simple shape.
See: RepRec pick and place robots and ReChain frame systems
Related
External links
- Wikipedia: Brownian ratchet
