Biological activity requires a solvent that can provide a suitable environment, which satisfies
the twin need for stability and the ability to change. Among all the solvents water plays the …

The functional structure of proteins results from marginally stable folded conformations.
Reversible unfolding, irreversible denaturation, and deterioration can be caused by …

Liquid-liquid phase separation (LLPS) can drive a multitude of cellular processes by
compartmentalizing biological cells via the formation of dense liquid biomolecular …

Liquid–liquid phase separation (LLPS) plays a key role in the compartmentalization of cells
via the formation of biomolecular condensates. Here, we combined atomistic molecular …

The total free energy of a hydrated biomolecule and its corresponding decomposition of
energy and entropy provides detailed information about regions of thermodynamic stability …

Characterization of the hydrated state of a protein is crucial for understanding its structural
stability and function. In the present study, we have investigated the 3D hydration structure of …

Of late, DESs have occupied the centre stage due to their eco-friendly and resource-efficient
nature and their low toxicity. In this work, we have investigated the structural and thermal …

The concept that a fluid has a position-dependent free energy density appears in the
literature but has not been fully developed or accepted. We set this concept on an …

Fluorine is an element renowned for its unique properties. Its powerful capability to modulate
molecular properties makes it an attractive substituent for protein binding ligands; however …

Peptides are promising therapeutic agents for various biological targets due to their high
efficacy and low toxicity, and the design of peptide ligands with high binding affinity to the …