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 …

Internal subnanosecond timescale motions are key for the function of proteins, and are
coupled to the surrounding solvent environment. These fast fluctuations guide protein …

In multicellular organisms, nucleosomes carry epigenetic information that defines distinct
patterns of gene expression, which are inherited over multiple generations. The enhanced …

Macromolecular crowding influences protein mobility and stability in vivo. A precise description
of the crowding effect on protein thermal stability requires the estimate of the combined …

Conformational changes occurring during the enzymatic turnover are essential for the regulation
of protein functionality. Individuating the protein regions involved in these changes and …

Comparing homologous enzymes adapted to different thermal environments aids to shed
light on their delicate stability/function trade-off. Protein mechanical rigidity was postulated to …

In this work, we combine experiments and molecular simulations to unveil the hidden allosteric
propensity of a thermophilic malate dehydrogenase protein (MDH). We provide evidence …

We introduce a novel strategy to quantify the disorder of extended water–water hydrogen-bond
(HB) networks sampled in particle-based computer simulations. The method relies on the …

Table S1: Conformational and kinetic clustering of the MD simulations. The conformational
clustering was based on the collective variable RMSD and using a cut-off of 2.5 Å. The total …

Our work focuses on determining the effect of crowded environment and different solvents
on the thermal stability of the protein Lysozyme [1] placed in a dilute water solution, …