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2016 | 63 | 1 | 65-70
Article title

Protein thermal stabilization in aqueous solutions of osmolytes

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Proteins' thermal stabilization is a significant problem in various biomedical, biotechnological, and technological applications. We investigated thermal stability of hen egg white lysozyme in aqueous solutions 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>NMG>TMAO≈DMG>TMG. Theoretical calculations (DFT) showed clearly that osmolytes' amino group protons and water molecules 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.
Physical description
  • Department of Physical Chemistry, Chemical Faculty, Gdansk University of Technology, Gdańsk, Poland
  • Department of Physical Chemistry, Chemical Faculty, Gdansk University of Technology, Gdańsk, Poland
  • Département de Chimie Moléculaire, CNRS UMR5250, ICMG FR2607, Université de Grenoble, 570 Grenoble Cedex 9, France
  • Department of Physical Chemistry, Chemical Faculty, Gdansk University of Technology, Gdańsk, Poland
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