Macromolecules in Solution

  • Peter R. Bergethon


We have already described the solvent-solute structure in aqueous solutions of small polar and non-polar molecules. The view of the disturbance of the normal hexagonal structure of liquid water by these small solutes can serve as a model for solutions of macromolecules, which, to a reasonable approximation, may be treated as a chain of small solute molecules attached to each other. Such molecules are polymers. Polymers of a single component or monomer are called homopolymers (A n ). Copolymers are composed of two or more monomers. Copolymers can be random (AAABBABBBA...) or ordered (ABABABAB or ABCABCABC). Polymers of these types are mainstays of the chemical industry, and their solubility or insolubility in aqueous environments can now be predicted with a high degree of accuracy, allowing us to properly formulate the polymerizing mixture.


Bovine Spongiform Encephalopathy Amyloid Fibril Denature State COOH COOH Fatal Familial Insomnia 
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Further Reading


  1. Sun S. F. (1994) Physical Chemistry of Macromolecules, Basic Principles and Issues. John Wiley and Sons, New York.Google Scholar
  2. Tanford C. (1961) Physical Chemistry of Macromolecules. John Wiley and Sons, New York.Google Scholar

Protein Folding

  1. Creighton T. E., ed. (1992) Protein Folding. W. H. Freeman and Company, New York.Google Scholar
  2. Dill K. A. (1985) Theory for the folding and stability of globular proteins. Biochemistry 24: 1501–9.PubMedCrossRefGoogle Scholar
  3. Elber R., and Karplus M. (1987) Multiple conformational states of proteins: A molecular dynamics analysis of myoglobin. Science 253: 318–21.CrossRefGoogle Scholar
  4. Fersht A. R., and Serrano L. (1993) Principles of protein stability derived from protein engineering experiments. Current Opinion in Structural Biology, 3: 7583.CrossRefGoogle Scholar
  5. Kim P. S., and Baldwin R. L. (1982) Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding. Ann. Rev. Biochem., 51: 459–89.PubMedCrossRefGoogle Scholar
  6. Matthew C. R. (1993) Pathways of protein folding. Ann. Rev. Biochem., 62: 653–83.CrossRefGoogle Scholar
  7. Richards F. M. (1991) The protein folding problem. Sci. Am., 264 (1): 54–63.PubMedCrossRefGoogle Scholar
  8. Rose G. D., and Wolfenden (1993) Hydrogen bonding, hydrophobicity, packing and protein folding. Ann. Rev. Biophys. Biomol. Struct., 22: 381–415.CrossRefGoogle Scholar
  9. Scholtz J. M., and Baldwin R. L. (1992) The mechanism of a-helix formation by peptides. Ann. Rev. Biophys. Biomol. Struct., 21: 95–118.CrossRefGoogle Scholar
  10. Shortle D. (1989) Probing the determinants of protein folding and stability with amino acid substitutions. J. Biol. Chem., 264: 5315–18.PubMedGoogle Scholar
  11. Shortle D. (1993) Denatured states of proteins and their roles in folding and stability. Current Opinion in Structural Biology, 3: 66–74.CrossRefGoogle Scholar
  12. Taubes G. (1996) Misfolding the way to disease. Science, 271: 1493–5.PubMedCrossRefGoogle Scholar
  13. Timasheff S. N. (1993) The control of protein stability and association by weak interactions with water: How do solvents affect these processes? Ann. Rev. Biophys. Biomol. Struct., 22: 67–97.CrossRefGoogle Scholar

The Amyloidoses

  1. Bergethon P. R., Sabin T. D., Lewis D., Simms R. W., Cohen A. S., and Skinner M. (1996) Improvement in the polyneuropathy associated with familial amyloid polyneuropathy after liver transplantation. Neurology, 47: 944–51.PubMedCrossRefGoogle Scholar
  2. Booth D. R., Sunde M., Bellotti V., Robinson C. V., Hutchinson W. L., Fraser P. E., Hawkins P. N., Dobson C. M., Radford S. E., Blake C. C. F., and Pepys M. B. (1997) Instability, unfolding and aggregation of human lysozyme varients underlying amyloid fibrillogenesis. Nature, 385: 787–93.PubMedCrossRefGoogle Scholar
  3. Eigen M. (1993) Viral quasi-species. Sci. Am., 269 (1): 42–49.PubMedCrossRefGoogle Scholar
  4. Kelly J. W., and Lansbury P. T. (1994) A chemical approach to elucidate the mechanism of transthyretin and (3-protein amyloid fibril formation. Amyloid: Int. J. Exp. Clin. Invest., 1: 186–205.Google Scholar
  5. Kemper T. L. (1994) Neuroanatomical and Neuropatho-logical Change During Aging and Dementia, in Clinical Neurology of Aging, 2d ed., Albert M. L., and Knoefel J. E., eds., 3–67. Oxford University Press, Oxford.Google Scholar
  6. Pepys M. B., Hawkins P. N., Booth D. R., Vigushin D. M., Tennent G. A., Soutar A. K., Totty N., Nguyent O., Blake C. C. F., Terry C. J., Feest T. G., Zahn A. M., and Hsuan J. J. (1993) Human lysozyme gene mutations cause hereditary systemic amyloidosis. Nature, 362: 553–7.PubMedCrossRefGoogle Scholar
  7. Perutz M. F. (1997) Mutations make enzyme polymerize. Nature, 385: 773–5.PubMedCrossRefGoogle Scholar
  8. Prusiner S. B., and DeArmond S. J. (1995) Prion protein amyloid and neurodegeneration. Amyloid: Int. J. Exp. Clin. Invest., 2: 39–65.Google Scholar
  9. Selkoe D. J. (1991) Amyloid protein and Alzheimer’s disease. Sci. Am., 265 (5): 68–78.PubMedCrossRefGoogle Scholar
  10. Steinhart C. (1996) Sick cows, protein geometry and politics. J. Chem. Ed., 73: A232–3.CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1998

Authors and Affiliations

  • Peter R. Bergethon
    • 1
  1. 1.Department of BiochemistryBoston University School of MedicineBostonUSA

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