Claudio J. Margulis

TL;DR: Molecular dynamics simulations of the collapse of a two-domain protein, the BphC enzyme, into a globular structure are performed to examine how water molecules mediate hydrophobic collapse of proteins.

TL;DR: This study investigates the slow dynamics of 1-butyl-3-methylimidazolium hexafluorophosphate, a very popular room-temperature ionic solvent and predicts the existence of heterogeneity in the liquid and shows that this heterogeneity is the underlying microscopic cause for the recently reported "red-edge effect" observed in the study of fluorescence of the organic probe 2-amino-7-nitrofluorene.

TL;DR: By understanding how S(q) changes as imidazolium-based ionic systems undergo solid-liquid phase transition, and by artificially perturbing the liquid structure in a way that directly couples to the intensity of the FSDP, its geometric origin is identified in a rigorous way.

TL;DR: This article explores in atomistic detail and explains in an intuitive way the peculiar volumetric behavior experimentally observed when supercritical CO2 is dissolved in 1-butyl-3-methylimidazolium hexafluorophosphate ([Bmim+] [PF6(-)] and proposes that CO2 occupies extremely well-defined locations in the IL.

TL;DR: The results that have been obtained indicate that distributed kinetics and dynamical heterogeneity may sometimes, but not always, be influencing factors in ionic liquids.