The stabilization of proteins by osmolytes
- 1 March 1985
- journal article
- research article
- Published by Elsevier BV in Biophysical Journal
- Vol. 47 (3), 411-414
- https://doi.org/10.1016/s0006-3495(85)83932-1
Abstract
The preferential interactions of lysozyme with solvent components and the effects of solvent additives on its stability were examined for several neutral osmolytes: L-proline, L-serine, gamma-aminobutyric acid, sarcosine, taurine, alpha-alanine, beta-alanine, glycine, betaine, and trimethylamine N-oxide. It was shown that all these substances stabilize the protein structure against thermal denaturation and (except for trimethylamine N-oxide for which interaction measurements could not be made) are strongly excluded from the protein domain, rendering unlikely their direct binding to proteins. On the other hand, valine, not known as an osmolyte, had no stabilizing effect, although it induced a large protein-preferential hydration. A possible explanation is given for the use of these substances as osmotic-pressure-regulating agents in organisms living under high osmotic pressure.Keywords
This publication has 16 references indexed in Scilit:
- Preferential interactions of proteins with salts in concentrated solutionsBiochemistry, 1982
- Stabilization of protein structure by sugarsBiochemistry, 1982
- Living with Water Stress: Evolution of Osmolyte SystemsScience, 1982
- Thermodynamic and kinetic examination of protein stabilization by glycerolBiochemistry, 1981
- Preferential and absolute interactions of solvent components with proteins in mixed solvent systemsPeptide Science, 1972
- Hydrogen ion titration curve of lysozyme in 6 M guanidine hydrochlorideBiochemistry, 1971
- Hydration of macromolecules. IV. Polypeptide conformation in frozen solutionsJournal of the American Chemical Society, 1971
- Protein hydrationArchives of Biochemistry and Biophysics, 1968
- Deoxyribonueleate solutions: Sedimentation in a density gradient, partial specific volumes, density and refractive index increments, and preferential interactionsPeptide Science, 1968
- The extrapolation of light-scattering data to zero concentrationArchives of Biochemistry and Biophysics, 1959