Dimer crystallization of chiral proteoids.

摘要: Proteins can self-assemble into a variety of exquisitely organized structures through hierarchical reaction pathways. To examine how different core shapes proteins and entropy combine to influence self-assembly, we create systems lithographically fabricated proteomimetic colloids, or 'proteoids', explore Brownian monolayers mobile proteoids, which have hard interactions, as they are slowly crowded. Remarkably, chiral C-shaped proteoids having circular heads on only one side form enantiopure lock-and-key dimers; these dimers corrugated, shape-complementary perimeters, so they, in turn, arrangements dimer crystals. Time-lapse video microscopy reveals the expulsion monomers from growing crystals tautomerization translocation reactions expedite crystallization kinetics. By mutating also tune types resulting Thus, rational design sub-particle features hard-core colloidal be used sterically select desired self-assembly pathways without introducing any site-specific attractions, thereby generating striking degree self-ordering, reminiscent protein crystallization.