Theory for the coalescence of viscous lenses

Drop coalescence occurs through the rapid growth of a liquid bridge that connects the two drops. At early times after contact, the bridge dynamics is typically self-similar, with details depending on the geometry and viscosity of the liquid. In this paper we analyse the coalescence of two-dimensional viscous drops that float on a quiescent deep pool; such drops are called liquid lenses. The analysis is based on the thin-sheet equations, which were recently shown to accurately capture experiments of liquid lens coalescence. It is found that the bridge dynamics follows a self-similar solution at leading order, but, depending on the large-scale boundary conditions on the drop, significant corrections may arise to this solution. This dynamics is studied in detail using numerical simulations and through matched asymptotics. We show that the liquid lens coalescence can involve a global translation of the drops, a feature that is confirmed experimentally.

Salt bridge dynamics in nonspecific protein/DNA binding: a comparative analysis of Elk1 and ETV6

Electrostatic protein/DNA interactions arise from the neutralization of the DNA phosphodiester backbone as well as coupled exchanges by charged protein residues as salt bridges or with mobile ions. Much focus...

Criticality in the conformational phase transition among self-similar groups in intrinsically disordered proteins: probed by salt-bridge dynamics

Intrinsically disordered proteins (IDP) serve as one of the key components in the global proteome. In contrast to the dominant class of cytosolic globular proteins, they harbor an enormous amount of physical flexibility and structural plasticity enforcing them to be retained in conformational ensembles rather than well defined stable folds. Previous studies in an aligned direction have revealed the importance of transient dynamical phenomena like that of saltbridge formation in IDPs to support their physical flexibility and have further highlighted their functional relevance. For this characteristic flexibility, IDPs remain amenable and accessible to different ordered binding partners, supporting their potential multi-functionality. The current study further addresses this complex structure-functional interplay in IDPs using phase transition dynamics to conceptualize the underlying (avalanche type) mechanism of their being distributed across and hopping around degenerate structural states (conformational ensembles). For this purpose, extensive molecular dynamics simulations have been done and the data analyzed from a statistical physics perspective. Investigation of the plausible scope ‘selforganized criticality’ (SOC) to fit into the complex dynamics of IDPs was found to be assertive, relating the conformational degeneracy of these proteins to their multi-functionality. In accordance with the transient nature of ‘salt-bridge dynamics’, the study further uses it as a probe to explain the structural basis of the proposed criticality in the conformational phase transition among self-similar groups in IDPs. The analysis reveal scale-invariant self-similar fractal geometries in structural conformations of different IDPs. Also, as discussed in the conclusion, the study has the potential to benefit structural tinkering of bio-medically relevant IDPs in the design of biotherapeutics against them.