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Molecular Basis of the Biological Compatibility of Nature’s Osmolytes

  • Conference paper
Book cover Transport Processes, Iono- and Osmoregulation

Part of the book series: Proceedings in Life Sciences ((LIFE SCIENCES))

Abstract

With the exception of halophilic bacteria, essentially all cells respond to a hyperosmotic stress with an accumulation of certain relatively nontoxic, organic solutes (Yancey et al. 1982; Jones et al. 1977; Costa and Pierce 1983). These compatible solutes or osmolytes have been shown by the speakers at this symposium and others to have unique properties which render them especially fit to serve as intracellular solutes. The purpose of this chapter is to review the fundamental reasons why some solutes (including those commonly used by nature) are “kind” to protein structures and functions and why others are not. While the original literature dealing with this topic relies heavily on thermodynamic arguments to describe protein-solute interactions, this review will attempt to treat the subject matter largely descriptively. In some cases, this requires an interpretation or simplification of thermodynamic observations which may not be totally accurate. However, it is hoped that the benefit of having a physical explanation of solute effects on protein structure will partially offset the disadvantage of not having a rigorous analysis of the various concepts.

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References

  • Arakawa T, Timasheff SN (1982) Preferential interaction of proteins with salts in concentrated solutions. Biochemistry 21:6545–6552

    Article  PubMed  CAS  Google Scholar 

  • Arakawa T, Timasheff SN (1982) Stabilization of protein structure by sugars. Biochemistry 21: 6536–6544

    Article  PubMed  CAS  Google Scholar 

  • Arakawa T, Timasheff SN (1983) Preferential interactions of proteins with solvent components in aqueous amino acid solutions. Arch Biochem Biophys 224:169–177

    Article  PubMed  CAS  Google Scholar 

  • Arakawa T, Timasheff SN (1984) The mechanism of action of Na glutamate, lysine HCl, and piperazine-N,N′bis(2-ethanesulfonic acid) in the stabilization of tubulin and microtubule formation. J Biol Chem 259:4979–4986

    PubMed  CAS  Google Scholar 

  • Back JF, Oakenfull LD, Smith MB (1979) Increased thermal stability of proteins in the presence of sugars and polyols. Biochemistry 18:5191 5196

    Google Scholar 

  • Clark ME, Burnell EE, Chapman NR, Hinke JAM (1982) Water in barnacle muscle. IV. Factors contributing to reduced self-diffusion. Biophys J 39:289–299

    Article  PubMed  CAS  Google Scholar 

  • Costa CJ, Pierce SK (1983) Volume regulation in the red coelomocytes of glycera dibranchiata: an interaction of amino acids and K+ effluxes. J Comp Physiol 151:133–144

    CAS  Google Scholar 

  • Gekko K, Koga S (1984) The stability of protein structure in aqueous prophylene glycol: amino acid solubility and preferential solvation of protein. Biochim Biophys Acta 786:151–160

    Article  CAS  Google Scholar 

  • Gekko K, Timasheff SN (1981) Mechanism of protein stabilization by glycerol: preferential hydration in glycerol-water mixtures. Biochemistry 20:4667–4676

    Article  PubMed  CAS  Google Scholar 

  • Gerlsma SY (1970) The effects of polyhydric and monohydric alcohols on the heat induced reversible denaturation of chymotrypsinogen A. Eur J Biochem 14:150–153

    Article  PubMed  CAS  Google Scholar 

  • Hamabata A, von Hippel PH (1973) Model studies on the effects of neutral salts on the conformational stability of biological macromolecules. II. Effects of vicinal hydrophobic groups on the specificity of binding of ions to amide groups. Biochemistry 12:1264–1271

    Article  PubMed  CAS  Google Scholar 

  • Hand SC, Somero GN (1982) Urea and methylamine effects on rabbit muscle phosphofructokinase: catalytic stability and aggregation state as a function of pH and temperature. J Biol Chem 257: 734–741

    PubMed  CAS  Google Scholar 

  • Herskovits TT, Gadegbeku B, Joillet H (1970) On the structural stability and solvent denaturation of proteins: I. denaturation by alcohols and glycols. J Biol Chem 245:2588–2598

    PubMed  CAS  Google Scholar 

  • Inoue H, Timasheff SN (1972) Preferential and absolute interactions of solvent components with proteins in mixed solvent systems. Biopolymers 11:737–743

    Article  PubMed  CAS  Google Scholar 

  • Jones RGW, Pollard A (1982) Towards a physical chemical characterization of compatible solutes. In: Franks F, Matthias R (eds) The biophysics of water. John Wiley, New York, p 335–339

    Google Scholar 

  • Jones RGW, Storey R, Leigh RA, Ahmad N, Pollard A (1977) A hypothesis on cytoplasmic osmoregulation. In: Morre E, Cifferi O (eds) Regulation of cell membrane activities in plants. Elsevier, Amsterdam, p 121

    Google Scholar 

  • Lee JC, Timasheff SN (1974) Partial specific volumes and interactions with solvent components of proteins in guanidine hydrochloride. Biochemistry 13:257–265

    Article  PubMed  CAS  Google Scholar 

  • McCall DW, Douglass DC (1965) The effect of ions on the self-diffusion of water: I. Concentration dependence. J Phys Chem 69:2001–2011

    Article  CAS  Google Scholar 

  • Melander W, Horvath C (1977) Salt effects on hydrophobic interactions in precipitation and chromatography of proteins: an interpretation of the lyotropic series. Arch Biochem Biophys 183: 200–215

    Article  PubMed  CAS  Google Scholar 

  • Prakash V, Loucheux C, Scheufele S, Gorbunoff MJ, Timasheff SN (1981) Interactions of proteins with solvent components in 8 M urea. Arch Biochem Biophys 210:455–464

    Article  PubMed  CAS  Google Scholar 

  • Shifrin S, Parrott CL (1975) Influence of glycerol and other polyhydric alcohols on the quaternary structure of an oligomeric protein. Arch Biochem Biophys 166:426–432

    Article  PubMed  CAS  Google Scholar 

  • Timasheff SN, Lee JC, Pittz EP, Tweedy N (1976) The interaction of tubulin and other proteins with structure-stabilizing solvents. J Colloid Interface Sci 55:658–663

    Article  CAS  Google Scholar 

  • von Hippel PH, Schleich T (1969) The effects of neutral salts on the structure and conformational stability of macromolecules in solution. In: Timasheff SN, Fasman GD (eds) Structure and stability of biological macromolecules. Dekker, New York, pp 417–574

    Google Scholar 

  • von Hippel PH, Peticolas V, Schack L, Karlson L (1973) Model studies on the effects of neutral salts on the conformational stability of biological macromolecules. I. Ion binding to Polyacrylamide and polystyrene columns. Biochemistry 12:1256–1264

    Article  Google Scholar 

  • Washburn EW (ed) (1928) International critical tables of numerical data, physics, chemistry and technology, vol IV. McGraw-Hill Book, New York, p 463

    Google Scholar 

  • Yancey PH, Somero GN (1978) Counteraction of urea destabilization of protein structure by methylamine osmoregulatory compounds of elasmobranch fishes. Biochem J 183:317–323

    Google Scholar 

  • Yancey PH, Clark ME, Hand SC, Bowlus RD, Somero GN (1982) Living with water stress: evolution of osmolyte systems. Science 217:1214–1222

    Article  PubMed  CAS  Google Scholar 

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© 1985 Springer-Verlag Berlin Heidelberg

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Low, P.S. (1985). Molecular Basis of the Biological Compatibility of Nature’s Osmolytes. In: Gilles, R., Gilles-Baillien, M. (eds) Transport Processes, Iono- and Osmoregulation. Proceedings in Life Sciences. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-70613-4_39

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  • DOI: https://doi.org/10.1007/978-3-642-70613-4_39

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-70615-8

  • Online ISBN: 978-3-642-70613-4

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