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Abstract
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.
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Authors (4)
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Muriel Jourdan
- Université de Grenoble Département de Chimie Moléculaire
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- Publication version
- Accepted or Published Version
- DOI:
- Digital Object Identifier (open in new tab) 10.18388/abp.2014_950
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Details
- Category:
- Articles
- Type:
- artykuł w czasopiśmie wyróżnionym w JCR
- Published in:
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Acta Biochimica Polonica
no. 63,
pages 65 - 70,
ISSN: 0001-527X - Language:
- English
- Publication year:
- 2016
- Bibliographic description:
- Bruździak P., Panuszko A., Jourdan M., Stangret J.: Protein thermal stabilization in aqueous solutions of osmolytes// Acta Biochimica Polonica. -Vol. 63, iss. 1 (2016), s.65-70
- DOI:
- Digital Object Identifier (open in new tab) 10.18388/abp.2014_950
- Verified by:
- Gdańsk University of Technology
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