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Bernat Durà Faulí

Publications and source records attributed to Bernat Durà Faulí.

2 recordsLinked to original sources

Slit-snapping and multistability in buckled beams with partial cuts

Elastic instabilities such as buckling and snapping have evolved into a powerful design principle, enabling memory, sequential shape morphing, and computing in metamaterials and devices. Modifying the post-buckling configurations or their snapping transitions would greatly expand design possibilities, yet general principles for controlling elastic instabilities are lacking. Here, we show that adding a partial cut, or slit, to a flexible beam enables precise control of post-buckling behavior: under compression, slit-beams first buckle, then snap, leading to trista-bility within the hysteretic regime. A truss model explains these phenomena by uncovering the interplay of geometric and slit induced nonlinearities. Leveraging these insights, we realize multi-slit beams with programmable behavior, unlocking a vast design space featuring giant hysteresis, quadstability, multi-step snapping, tristability at zero compression, and compression-induced snapping between left and right-buckled states. Our strategy is general, simple to design and implement, and enables mechanical metamaterials and devices with advanced memory and sequential behavior.

cond-mat.soft↗

Hydrophobic homopolymer's coil-globule transition and adsorption onto a hydrophobic surface under different conditions

Unstructured proteins can modulate cellular responses to environmental conditions by undergoing coil-globule transitions and phase separation. However, the molecular mechanisms of these phenomena still need to be fully understood. Here, we use Monte Carlo calculations of a coarse-grained model incorporating water's effects on the system's free energy. Following previous studies, we model an unstructured protein as a polymer chain. Because we are interested in investigating how it responds to thermodynamic changes near a hydrophobic surface under different conditions, we choose an entirely hydrophobic sequence to maximize the interaction with the interface. We show that a slit pore confinement without top-down symmetry enhances the unfolding and adsorption of the chain in both random coil and globular states. Moreover, we demonstrate that the hydration water modulates this behavior depending on the thermodynamic parameters. Our findings provide insights into how homopolymers, and possibly unstructured proteins, can sense and adjust to external stimuli such as nanointerfaces or stresses.

cond-mat.soft↗