The interactions of water with the various functional groups of proteins play crucial role in determining the conformational stability of proteins. The interactions between charged biomolecules and ions can highly influence the behavior and conformation of former molecules in aqueous solutions and study of these interactions do provide an insight into their conformational stability and unfolding behavior. As the amino acids in vivo are not involved in pure aqueous medium, their studies in the presence of various electrolytes, non-electrolytes, zwitterions i.e. molecules of various sizes, shapes and characteristics, like polarity and hydrophobicity are much in place. Partial molar quantities and the transfer functions determined at infinite dilution are extremely useful in the elucidation of mutual interactions between amino acid and cosolute/cosolvent molecules.