PMID: 11325420Apr 28, 2001Paper

Effects of water activity and aqueous solvent ordering on thermal stability of lysozyme, alpha-chymotrypsinogen A, and alcohol dehydrogenase

International Journal of Biological Macromolecules
S MatsueO Miyawaki

Abstract

Effects of water activity (aW) and solvent ordering were separately analyzed on the thermal unfolding of lysozyme and alpha-chymotrypsinogen A, and also on the thermal deactivation of yeast alcohol dehydrogenase (YADH) in aqueous solutions with various additives. With the coexistence of additives, water activity was the determinant of the extent of the change in the thermal stability of proteins while solvent ordering was the determinant of the direction of the change. The parameter alpha, determined from the activity coefficient of water, representing the deviation of aW from that of the ideal solution, was useful as a quantitative index of the solvent ordering showing good correlations with the unfolding temperature and enthalpy of lysozyme and alpha-chymotrypsinogen A and also with the thermal deactivation rate constant of YADH at a constant aW. Solvent ordering seemed to affect the thermal stability of proteins mainly through its effect on the intramolecular hydrophobic interaction among amino acid residues in a protein molecule but the contribution of the electrostatic interaction including hydrogen bonding through the change in permittivity of solution was also suggested.

References

Jul 20, 1992·Journal of Molecular Biology·G I Makhatadze, P L Privalov
Aug 15, 1990·The Biochemical Journal·M M Kristjansson, J E Kinsella
Mar 1, 1989·Proceedings of the National Academy of Sciences of the United States of America·M K Gilson, B Honig
Jan 1, 1988·Advances in Protein Chemistry·P L Privalov, S J Gill
Sep 1, 1984·Proceedings of the National Academy of Sciences of the United States of America·B H Honig, W L Hubbell
Sep 1, 1981·Archives of Biochemistry and Biophysics·V PrakashS N Timasheff
May 26, 1995·Science·B Honig, A Nicholls
Feb 28, 1997·Biophysical Chemistry·G Xie, S N Timasheff
Jun 1, 1997·Protein Science : a Publication of the Protein Society·C Tanford
Jan 1, 1959·Advances in Protein Chemistry·W KAUZMANN

❮ Previous
Next ❯

Citations

Sep 13, 2002·Bioscience, Biotechnology, and Biochemistry·Hitomi KumagaiHitoshi Kumagai
Mar 9, 2005·Biochimica Et Biophysica Acta·Hidehiko HirakawaTeruyuki Nagamune
Jun 5, 2020·International Journal of Biological Macromolecules·Timur MagsumovIgor Sedov
Mar 19, 2011·Journal of Agricultural and Food Chemistry·Pablo A SobralJorge R Wagner
Sep 21, 2017·Bioconjugate Chemistry·Yijia XiongThomas C Squier
Oct 29, 2008·International Journal of Biological Macromolecules·Adak NasiripourdoriKhosro Khajeh
Jan 1, 2010·Colloids and Surfaces. B, Biointerfaces·Marina C CrescimbeniMaría A Perillo

❮ Previous
Next ❯

Related Concepts

Related Feeds

Bacterial Cell Wall Structure (ASM)

Bacterial cell walls are made of peptidoglycan (also called murein), which is made from polysaccharide chains cross-linked by unusual peptides containing D-amino acids. Here is the latest research on bacterial cell wall structures.

Bacterial Cell Wall Structure

Bacterial cell walls are made of peptidoglycan (also called murein), which is made from polysaccharide chains cross-linked by unusual peptides containing D-amino acids. Here is the latest research on bacterial cell wall structures.