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At zero temperature, spring networks with connectivity below Maxwell's isostatic threshold undergo a mechanical phase transition from a floppy state at small strains to a rigid state for applied shear strain above a critical strain threshold. Disordered networks in the floppy mechanical regime can be stabilized by entropic effects at finite temperature. We develop a scaling theory for this mechanical phase transition at finite temperature, yielding relationships between various scaling exponents. Using Monte Carlo simulations, we verify these scaling relations and identify anomalous entropic elasticity with sublinear 𝑇 dependence in the linear elastic regime. While our results are consistent with prior studies of phase behavior near the isostatic point, the present work also makes predictions relevant to the broad class of disordered thermal semiflexible polymer networks for which the connectivity generally lies far below the isostatic threshold. 

Fibrous networks such as collagen are common in physiological systems. One important function of these networks is to provide mechanical stability for cells and tissues. At physiological levels of connectivity, such networks would be mechanically unstable with only central-force interactions. While networks can be stabilized by bending interactions, it has also been shown that they exhibit a critical transition from floppy to rigid as a function of applied strain. Beyond a certain strain threshold, it is predicted that underconstrained networks with only central-force interactions exhibit a discontinuity in the shear modulus. We study the finite-size scaling behavior of this transition and identify both the mechanical discontinuity and critical exponents in the thermodynamic limit. We find both non-mean-field behavior and evidence for a hyperscaling relation for the critical exponents, for which the network stiffness is analogous to the heat capacity for thermal phase transitions. Further evidence for this is also found in the self-averaging properties of fiber networks. 

Networks of filamentous actin (F-actin) are important for the mechanics of most animal cells. These cytoskeletal networks are highly dynamic, with a variety of actin-associated proteins that control cross-linking, polymerization and force generation in the cytoskeleton. Inspired by recent rheological experiments on reconstituted solutions of dynamic actin filaments, we report a theoretical model that describes stress relaxation behavior of these solutions in the presence of severing proteins. We show that depending on the kinetic rates of assembly, disassembly, and severing, one can observe both length-dependent and length-independent relaxation behavior.