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. 1985 Mar;47(3):411–414. doi: 10.1016/S0006-3495(85)83932-1

The stabilization of proteins by osmolytes.

T Arakawa, S N Timasheff
PMCID: PMC1435219  PMID: 3978211

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Arakawa T., Timasheff S. N. Preferential interactions of proteins with salts in concentrated solutions. Biochemistry. 1982 Dec 7;21(25):6545–6552. doi: 10.1021/bi00268a034. [DOI] [PubMed] [Google Scholar]
  2. Arakawa T., Timasheff S. N. Preferential interactions of proteins with solvent components in aqueous amino acid solutions. Arch Biochem Biophys. 1983 Jul 1;224(1):169–177. doi: 10.1016/0003-9861(83)90201-1. [DOI] [PubMed] [Google Scholar]
  3. Arakawa T., Timasheff S. N. Stabilization of protein structure by sugars. Biochemistry. 1982 Dec 7;21(25):6536–6544. doi: 10.1021/bi00268a033. [DOI] [PubMed] [Google Scholar]
  4. Bull H. B., Breese K. Protein hydration. I. Binding sites. Arch Biochem Biophys. 1968 Nov;128(2):488–496. doi: 10.1016/0003-9861(68)90055-6. [DOI] [PubMed] [Google Scholar]
  5. Cohen G., Eisenberg H. Deoxyribonucleate solutions: sedimentation in a density gradient, partial specific volumes, density and refractive index increments, and preferential interactions. Biopolymers. 1968;6(8):1077–1100. doi: 10.1002/bip.1968.360060805. [DOI] [PubMed] [Google Scholar]
  6. Gekko K., Morikawa T. Preferential hydration of bovine serum albumin in polyhydric alcohol-water mixtures. J Biochem. 1981 Jul;90(1):39–50. doi: 10.1093/oxfordjournals.jbchem.a133468. [DOI] [PubMed] [Google Scholar]
  7. Gekko K., Timasheff S. N. Thermodynamic and kinetic examination of protein stabilization by glycerol. Biochemistry. 1981 Aug 4;20(16):4677–4686. doi: 10.1021/bi00519a024. [DOI] [PubMed] [Google Scholar]
  8. Inoue H., Timasheff S. N. Preferential and absolute interactions of solvent components with proteins in mixed solvent systems. Biopolymers. 1972;11(4):737–743. doi: 10.1002/bip.1972.360110402. [DOI] [PubMed] [Google Scholar]
  9. Kuntz I. D. Hydration of macromolecules. IV. Polypeptide conformation in frozen solutions. J Am Chem Soc. 1971 Jan 27;93(2):516–518. doi: 10.1021/ja00731a037. [DOI] [PubMed] [Google Scholar]
  10. Kuntz I. D., Jr, Kauzmann W. Hydration of proteins and polypeptides. Adv Protein Chem. 1974;28:239–345. doi: 10.1016/s0065-3233(08)60232-6. [DOI] [PubMed] [Google Scholar]
  11. Lee J. C., Gekko K., Timasheff S. N. Measurements of preferential solvent interactions by densimetric techniques. Methods Enzymol. 1979;61:26–49. doi: 10.1016/0076-6879(79)61005-4. [DOI] [PubMed] [Google Scholar]
  12. Lee J. C., Timasheff S. N. The stabilization of proteins by sucrose. J Biol Chem. 1981 Jul 25;256(14):7193–7201. [PubMed] [Google Scholar]
  13. Roxby R., Tanford C. Hydrogen ion titration curve of lysozyme in 6 M guanidine hydrochloride. Biochemistry. 1971 Aug 31;10(18):3348–3352. doi: 10.1021/bi00794a005. [DOI] [PubMed] [Google Scholar]
  14. TIMASHEFF S. N., KRONMAN M. J. The extrapolation of light-scattering data to zero concentration. Arch Biochem Biophys. 1959 Jul;83(1):60–75. doi: 10.1016/0003-9861(59)90010-4. [DOI] [PubMed] [Google Scholar]
  15. WYMAN J., Jr LINKED FUNCTIONS AND RECIPROCAL EFFECTS IN HEMOGLOBIN: A SECOND LOOK. Adv Protein Chem. 1964;19:223–286. doi: 10.1016/s0065-3233(08)60190-4. [DOI] [PubMed] [Google Scholar]
  16. Yancey P. H., Clark M. E., Hand S. C., Bowlus R. D., Somero G. N. Living with water stress: evolution of osmolyte systems. Science. 1982 Sep 24;217(4566):1214–1222. doi: 10.1126/science.7112124. [DOI] [PubMed] [Google Scholar]

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