Condensed Matter Theory

Abstract:

We analyze in depth an S 3 -invariant nearest-neighbor quantum chain in the region of a U ( 1 ) -invariant self-dual multicritical point. We find four distinct proximate gapped phases. One has three-state Potts order, corresponding to topological order in a parafermionic formulation. Another has “representation” symmetry-protected topological (RSPT) order, while its dual exhibits an unusual “not- A ” order, where the spins prefer to align in two of the three directions. Within each of the four phases, we find a frustration-free point with exact ground state(s). The exact ground states in the not- A phase are product states, each an equal-amplitude sum over all states where one of the three spin states on each site is absent. Their dual, the RSPT ground state, is a matrix product state similar to that of Affleck-Kennedy-Lieb-Tasaki. A field-theory analysis shows that all transition lines are in the universality class of the critical three-state Potts model. They provide a lattice realization of a flow from a free-boson field theory to the Potts conformal field theory.

Abstract:

Many functional units in biology, such as enzymes or molecular motors, are composed of several subunits that can reversibly assemble and disassemble. This includes oligomeric proteins composed of several smaller monomers, as well as protein complexes assembled from a few proteins. By studying the generic spatial transport properties of such proteins, we investigate here whether their ability to reversibly associate and dissociate may confer on them a functional advantage with respect to nondissociating proteins. In uniform environments with position-independent association-dissociation, we find that enhanced diffusion in the monomeric state coupled to reassociation into the functional oligomeric form leads to enhanced reactivity with localized targets. In nonuniform environments with position-dependent association-dissociation, caused by, for example, spatial gradients of an inhibiting chemical, we find that dissociating proteins generically tend to accumulate in regions where they are most stable, a process that we term "stabilitaxis."