Macromolecules and Salts: Interactions

Abstract

Biological macromolecules carry electrical charges and operate in crowded and complex systems. An understanding of electrostatic interactions is essential for the evaluation of biological function.

Keywords: viscosity; analytical centrifugation; light scattering; X‐Ray scattering; neutron scattering; charged macromolecule–cosolvent interactions; protein–nucleic acid interactions

Figure 1.

(a) Viscosity numbers ηsp/c of E. coli RNA solutions at various NaCl concentrations (marked on each curve) at 25°C. (b) Intrinsic viscosities [η] of RNA solutions as a function of NaCl concentration. From Littauer and Eisenberg, , with permission.

Figure 2.

Second virial coefficients A2 (from light scattering) of poly(A), as a function of temperature; blue circles, 1740 nucleotides, 1 mol L−1 NaCl; green circles, 1462 nucleotides, 1 mol L−1 NaCl; red circles, 1740 nucleotides, 1.3 mol L−1 NaCl. From Eisenberg and Felsenfeld, , with permission.

Figure 3.

Relative light scattering intensities versus time in the denaturation process of halophilic malate dehydrogenase complexed with the coenzyme NADH in 0.8 mol L−1 NaCl, 5 mmol L−1 Tris, pH 8, 20°C. Insert: determination of translational coefficient D by dynamic light scattering distribution of particle sizes after (a) 1 h, (b) 24 h and (c) 118 h. From Bonneté et al., , with permission.

Figure 4.

Unsmoothed derivative plot of dA280/dr versus r of native and denatured halophilic malate dehydrogenase (hMDH) complexed with the coenzyme NADH after 120 min velocity sedimentation in 1.25 mol L−1 NaCl, 5 mol L−1 Tris, pH 8, 42 000 rpm, 20°C. From Bonneté et al., , with permission.

Figure 5.

Complementary superposition of normalized (*) data from equilibrium sedimentation, SAXS and SANS of halophilic malate dehydrogenase; (∂ρ/∂c2)μ* M2 versus ρx*. In NaCl: open circles, from densimetry; open squares, +, from s/D; ×, from equilibrium sedimentation; open diamonds, from SAXS; open triangles, from SANS. In KCl: closed squares, from equilibrium sedimentation; closed circles, from s/D; closed triangles, from SANS. Insert: enlargement of the lower part of the plot mass and X‐ray data). From Bonneté et al., , with permission.

Figure 6.

Schematic representation of the crystal structure of halophilic malate dehydrogenase from Haloarcula marismortui at 3.2 Å resolution. The numbers 1–4 correspond to the four monomers. Red spheres, acidic amino acids; blue spheres, basic amino acids. From Dym et al., , with permission.

close

References

Bonneté F, Ebel C, Zaccai G and Eisenberg H (1993) A biophysical study of halophilic malate dehydrogenase in solution, revised subunit structure and solvent interactions of native and recombinant enzyme. Journal of the Chemical Society, Faraday Transactions 89: 2659–2666.

Casassa EF and Eisenberg H (1964) Thermodynamic analysis of multicomponent solutions. Advances in Protein Chemistry 19: 287–395.

Dym O, Mevarech M and Sussman JL (1995) Structural features that stabilize halophilic malate dehydrogenase from an archaebacterium. Science 267: 1344–1346.

Eisenberg H (1976) Biological Macromolecules and Polyelectrolytes in Solution. Oxford: Clarendon Press.

Eisenberg H (1994) Protein and nucleic acid hydration and cosolvent interactions: establishment of reliable base‐line values at high cosolvent concentrations. Biophysical Chemistry 53: 57–68.

Eisenberg H (1995) Life in unusual environments: progress in understanding the structure and function of enzymes from extreme halophilic bacteria. Archives of Biochemistry and Biophysics 318: 1–5.

Eisenberg H (1998) Polyelectrolyte excluded volume and expansion, compared to non‐ionic polymers. Acta Polymerica 49: 534–538.

Eisenberg H and Felsenfeld G (1967) Studies of the temperature dependent conformation and phase separation of polyriboadenylic acid solutions at neutral pH. Journal of Molecular Biology 30: 17–37.

Flory PJ (1953) Principles of Polymer Chemistry. Ithaca, NY: Cornell University Press.

Fujita H (1994) Notes on the derivation of the sedimentation equilibrium equation. In: Schuster TM and Laue TM (eds) Modern Analytical Ultracentrifugation, pp. 3–14. Boston: Birkhäuser.

Jaenicke R and Böhm G (1998) The stability of proteins in extreme environments. Current Opinion in Structural Biology 8: 738–748.

Laue TM and Stafford III WF (1999) Modern applications of analytical ultracentrifugation. Annual Reviews of Biophysics and Biomolecular Structure 28: 75–100.

Littauer UZ and Eisenberg H (1959) Ribonucleic acid from Escherichia coli: preparation, characterization and physical properties. Biochimica Biophysica Acta 32: 320–337.

Mandel M (1988) Polyelectrolytes. In: Mark HF, Bikales NM, Overberger CG, Menges G and Kroschwitz JI (eds) Encyclopedia of Polymer Science and Engineering, 2nd edn. vol. 11, pp. 739–829. New York: Wiley.

McFail‐Isom L, Sines CC and Williams LD (1999) DNA structure: cations in charge? Current Opinion in Structural Biology 9: 298–304.

Mevarech M, Frolow F and Gloss L (2000) Halophilic enzymes: proteins with a grain of salt. Biophysical Chemistry 86: 155–164.

Record MT Jr, Zhang W and Anderson CF (1998) Analysis of effects of salts and uncharged solutes on protein and nucleic acids equilibria and processes: a practical guide to recognizing and interpreting polyelectrolyte effects, Hofmeister effects, and osmotic effects of salts. Advances in Protein Chemistry 51: 282–353.

Schellman JA (1994) The thermodynamics of solvent exchange. Biopolymers 34: 1015–1026.

Sharp KA and Honig B (1995) Salt effects on nucleic acids. Current Opinion in Structural Biology 5: 323–328.

Timasheff SN (1998) Control of protein stability and reactions by weakly interacting cosolvents: the simplicity of the complicated. Advances in Protein Chemistry 51: 355–432.

Warshel A and Papazyan A (1998) Electrostatic effects in macromolecules: fundamental concepts and practical modeling. Current Opinion in Structural Biology 8: 211–217.

Wyman J, Jr and Gill SJ (1990) Binding and Linkage. Functional Chemistry of Biological Macromolecules. Mill Valley, CA: University Science Books.

Further Reading

Casassa EF and Eisenberg H (1964) Thermodynamic analysis of multicomponent solutions. Advances in Protein Chemistry 19: 287–395.

Eisenberg H (1976) Biological Macromolecules and Polyelectrolytes in Solution. Oxford: Clarendon Press.

Flory PJ (1953) Principles of Polymer Chemistry. Ithaca, NY: Cornell University Press.

Jaenicke R and Böhm G (1998) The stability of proteins in extreme environments. Current Opinion in Structural Biology 8: 738–748.

Laue TM and Stafford III WF (1999) Modern applications of analytical ultracentrifugation. Annual Reviews of Biophysics and Biomolecular Structure 28: 75–100.

Mandel M (1988) Polyelectrolytes. In: Mark HF, Bikales NM, Overberger CG, Menges G and Kroschwitz JI (eds) Encyclopedia of Polymer Science and Engineering, 2nd edn. vol. 11, pp. 739–829. New York: Wiley.

McFail‐Isom L, Sines CC and Williams LD (1999) DNA structure: cations in charge? Current Opinion in Structural Biology 9: 298–304.

Record MT Jr, Zhang W and Anderson CF (1998) Analysis of effects of salts and uncharged solutes on protein and nucleic acids equilibria and processes: a practical guide to recognizing and interpreting polyelectrolyte effects, Hofmeister effects, and osmotic effects of salts. Advances in Protein Chemistry 51: 282–353.

Sharp KA and Honig B (1995) Salt effects on nucleic acids. Current Opinion in Structural Biology 5: 323–328.

Timasheff SN (1998) Control of protein stability and reactions by weakly interacting cosolvents: the simplicity of the complicated. Advances in Protein Chemistry 51: 355–432.

Warshel A and Papazyan A (1998) Electrostatic effects in macromolecules: fundamental concepts and practical modeling. Current Opinion in Structural Biology 8: 211–217.

Wyman J Jr and Gill SJ (1990) Binding and Linkage. Functional Chemistry of Biological Macromolecules. Mill Valley, CA: University Science Books.

Contact Editor close
Submit a note to the editor about this article by filling in the form below.

* Required Field

How to Cite close
Eisenberg, Henryk(Apr 2001) Macromolecules and Salts: Interactions. In: eLS. John Wiley & Sons Ltd, Chichester. http://www.els.net [doi: 10.1038/npg.els.0003118]