Micron-sized anisotropic particles with homogeneous surface properties at a fluid interface can deform the interface due to their shape. The particles thereby create excess interfacial area and interact in order to minimize this area, which lowers the total interfacial energy. We present a systematic investigation of the interface deformations around single ellipsoidal particles and cuboidal particles with rounded edges in the near field for various contact angles and particle aspect ratios. The correlation of these deformations with capillary bond energies-the interaction energies of two particles at contact-quantifies the relation between the interactions and the near-field deformations. We characterize the interactions using effective power laws and investigate how anisotropic particles self-assemble by capillary forces. Interface deformations and particle interactions for cuboidal particles are weaker compared with those for ellipsoidal particles with the same aspect ratios. For both particle shapes, the bound state in side-by-side orientation is most stable, while the interaction in tip-to-side orientation is repulsive. Furthermore, we find capillary attraction between spherical and ellipsoidal particles. Our calculations therefore suggest cluster formation of spherical and ellipsoidal particles, which elucidates the role of spherical particles as stoppers for the growth of worm-like chains of ellipsoidal particles. The interaction between spherical and ellipsoidal particles might also explain the suppression of the "coffee-ring effect" that has been observed for evaporating droplets with mixtures of spherical and ellipsoidal particles. In general, our calculations of the near-field interactions complement previous calculations in the far field and help to predict colloidal assembly and rheological properties of particle-laden interfaces.

Internal subnanosecond timescale motions are key for the function of proteins, and are coupled to the surrounding solvent environment. These fast fluctuations guide protein conformational changes, yet their role for protein stability, and for unfolding, remains elusive. Here, in analogy with the Lindemann criterion for the melting of solids, we demonstrate a common scaling of structural fluctuations of lysozyme protein embedded in different environments as the thermal unfolding transition is approached. By combining elastic incoherent neutron scattering and advanced molecular simulations, we show that, although different solvents modify the protein melting temperature, a unique dynamical regime is attained in proximity of thermal unfolding in all solvents that we tested. This solvation shell-independent dynamical regime arises from an equivalent sampling of the energy landscape at the respective melting temperatures. Thus, we propose that a threshold for the conformational entropy provided by structural fluctuations of proteins exists, beyond which thermal unfolding is triggered.