Département de chimie moléculaire

Proteins' thermal stabilization is a significant problem in various biomedical, biotechnol., and technol. applications. We investigated thermal stability of hen egg white lysozyme in aq. solns. of the following stabilizing osmolytes: Glycine (GLY), N-methylglycine (NMG), N,N-dimethylglycine (DMG), N,N,N-trimethylglycine (TMG), and trimethyl-N-oxide (TMAO). Results of CD-UV spectroscopic investigation were compared with FTIR hydration studies' results. Selected osmolytes increased lysozyme's thermal stability in the following order: Gly{\textgreater}NMG{\textgreater}TMAO≈DMG{\textgreater}TMG. Theor. calcns. (DFT) showed clearly that osmolytes' amino group protons and water mols. interacting with them played a distinctive role in protein thermal stabilization. The results brought us a step closer to the exact mechanism of protein stabilization by osmolytes. [on SciFinder(R)]