Published Paper Details:

Essential for life, proteins serve many purposes inside different organisms. But environmental factors sometimes provide major obstacles that affect protein solubility and structure. In response to such environmental challenges as temperature fluctuations, dehydration, and excessive salt or urea concentrations, cells gather tiny molecules known as osmolytes to assist proteins. This review is mostly about how these osmolytes change the stability and solubility of proteins by interacting with specific parts of proteins, like the backbone and side chains of amino acids. We investigate the thermodynamic ideas guiding these interactions, with particular attention to the idea of free energy transfer. Grounded in biophysical chemistry, the review assesses the predictive potential of the transfer model by analyzing protein transitions between folded (native) and unfolded (denatured). This method allows for the prediction of m-values, which are experimental measurements that gauge the effects of osmolytes on protein stability. Proteins tend to fold when urea interacts positively with their backbones. On the other hand, stabilizing osmolytes often interact negatively with protein backbones, which also moves proteins towards a folded state. While improving solubility, moderate stabilizers such as glycerol and proline maintain equilibrium with the fewest alterations to protein stability. This review generalizes the mechanism overview between osmolytes and Proteins.