The mechanism of protein stabilization by zwitterionic osmolytes has remained a long-
standing puzzle. While osmolytes are prevalently hypothesized to stabilize proteins by …

Thermoresponsive polymers (TRPs) in different solvent media have been studied over a
long period and are important from both scientific and technical points of view. Despite …

Trimethylamine-N-oxide (TMAO) and urea are commonly produced in many extremophilic
microorganisms that live in harsh environments. In view of high temperature, high pressure …

Choosing an appropriate collective variable (CV) for any biomolecular process is a
challenging task. Researchers are developing methods to solve this issue using a variety of …

The molecular mechanism of osmolytes on the stabilization of native states of protein is still
controversial irrespective of extensive studies over several decades. Recent investigations …

Osmolytes' mechanism of protecting proteins against denaturation is a longstanding puzzle,
further complicated by complex diversities inherent in protein sequences. An emergent …

The folding/unfolding equilibrium of proteins in aqueous medium can be altered by adding
small organic molecules generally termed as co-solvents. Denaturants such as urea are …

A detailed knowledge of hydrophobic association and solvation is crucial for understanding
the con-formational stability of proteins and polymers in osmolyte solutions. Using molecular …

In the recent surge of investigations on osmolyte-induced conformational landscape of
hydrophobic macromolecules notwithstanding, there is a lack of understanding of how the …

In the present study, we investigate the interaction of amino acid osmolytes, Arg, Lys, Asp
and Glu, and a denaturant, guanidinium chloride (Gdm) with proteins. To achieve this …