What Sustains Life? An Overview


The physicist looks at the expanding universe, disassembling toward disorder, and views increasing disorder as the inevitable flow in nature. The chemist burns the oils that have accumulated over the millennia in the earth’s crust and energizes molecules to react. On a smaller scale, the chemist sees the march toward disorder; the oils become dispersed and disordered gases, and the excited new molecules become dormant. Both physicists and chemists look at living organisms—propagating, assembling, growing—and wonder, how can living matter act in such an inverse way to the nonliving matter of their experiences? On the other hand, biochemists and biophysicists look at molecular systems of a dissected organism and successfully describe a still functional component in terms of the equilibrium laws of physics and chemistry. So, how can living matter seem so different from nonliving matter?


Energy Input Energy Conversion Chemical Energy Model Protein Mechanical Work 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    D.W. Urry, “Elastic Biomolecular Machines: Synthetic Chains of Amino Acids, Patterned After Those in Connective Tissue, Can Transform Heat and Chemical Energy into Motion.” Sci. Am. January 1995, 64–69.Google Scholar
  2. 3.
    C.B. Anfinsen, “Principles that Govern the Folding of Protein Chains.” Science, 181, 223–230, 1973.PubMedCrossRefGoogle Scholar
  3. 4.
    D.W. Urry, “Protein Folding and the Movements of Life.” The World & I, (Natural Science, At The Edge), 6, 301–309, 1991.Google Scholar
  4. 5.
    A. Szent-Györgyi, “Studies on Muscle.” Acta Physiol. Scand., 9 (suppl XXV), 1–116, 1945.Google Scholar
  5. 6.
    D.W. Urry, “Molecular Machines: How Motion and Other Functions of Living Organisms Can Result from Reversible Chemical Changes.” Angew. Chem. (German) 105, 859–883, 1993; Angew. Chem. Int. Ed. Engl., 32, 819–841, 1993.CrossRefGoogle Scholar
  6. 7.
    D.W. Urry, “Physical Chemistry of Biological Free Energy Transduction as Demonstrated by Elastic Protein-based Polymers” invited Feature Article, J. Phys. Chem. B, 101, 11007–11028, 1997.CrossRefGoogle Scholar
  7. 8.
    C.S. Roy, “The elastic properties of the arterial wall.” J. Physiol., 3, 125–159, 1880.Google Scholar
  8. 9.
    D.W. Urry and T.M. Parker, “Mechanics of Elastin: Molecular Mechanism of Biological Elasticity and its Relevance to Contraction.” J. Muscle Res. Cell Motil., 23, 541–557, 2002; Special Issue, Mechanics of Elastic Biomolecules. H. Granzier, M. Kellermayer, W. Linke, Eds.CrossRefGoogle Scholar
  9. 10.
    L.B. Sandberg, N.T. Soskel, and J.B. Leslie, “Elastin Structure, Biosynthesis and Relation to Disease States.” N. Engl. J. Med., 304, 566–579, 1981.PubMedCrossRefGoogle Scholar
  10. 11.
    H. Yeh, N. Ornstein-Goldstein, Z. Indik, P. Sheppard, N. Anderson, J.C. Rosenbloom, G. Cicila, K. Yoon, and Rosenbloom “Sequence Variation of Bovine Elastin mRNA Due to Alternative Splicing.” J. Collagen Rel. Res., 7, 235–247, 1987.Google Scholar
  11. 13.
    D.W. Urry, T. Hugel, M. Seitz, H. Gaub, L. Sheiba, J. Dea, J. Xu, and T. Parker “Elastin: A Representative Ideal Protein Elastomer.” Philos. Trans. R. Soc. Lond. B, 357, 169–184, 2002.CrossRefGoogle Scholar
  12. 14.
    D.W. Urry, T. Hugel, M. Seitz, H. Gaub, L. Sheiba, J. Dea, J. Xu, L. Hayes, F. Prochazka, and T. Parker, “Ideal Protein Elasticity: The Elastin Model.” In Elastomeric Proteins: Structures, Biomechanical Properties and Biological Roles. P.R. Shewry, A.S. Tatham, and A.J. Bailey, Eds. Cambridge University Press, The Royal Society; Chapter Four, pages 54–93, 2003.Google Scholar
  13. 15.
    E.O. Wilson, Consilience: The Unity of Knowledge. Alfred E. Knopf, New York, 1998, p. 8.Google Scholar
  14. 16.
    D.W. Urry, M.M. Long, and H. Sugano, “Cyclic Analog of Elastin Polyhexapeptide Exhibits an Inverse Temperature Transition Leading to Crystallization.” J. Biol. Chem., 253, 6301–6302, 1978.PubMedGoogle Scholar
  15. 17.
    M.V. Stackelberg and H.R. Müller, “Zur Struktur der Gashydrate.” Naturwissenschaften, 38, 456–458, 1951.CrossRefGoogle Scholar
  16. 18.
    D.W. Urry, S.Q. Peng, J. Xu, and D.T. McPherson, “Characterization of Waters of Hydrophobic Hydration by Microwave Dielectric Relaxation.” J. Am. Chem. Soc., 119, 1161–1162, 1997.CrossRefGoogle Scholar
  17. 20.
    E. Schrödinger, What is Life? Cambridge University Press, Cambridge, England, first published in 1944, Canto edition with “Mind and Matter” and Autobiographical Sketches, Forward by R. Penrose, 1992.Google Scholar
  18. 22.
    J.A.V. Butler, “The Energy and Entropy of Hydration of Organic Compounds.” Trans. Faraday Soc., 33, 229–238, 1937.CrossRefGoogle Scholar
  19. 24.
    For more details, see, for example, D. Voet, J.G. Voet, and C.W. Pratt, Fundamentals of Biochemistry. John Wiley & Sons New York, 1999, pp. 529–561.Google Scholar
  20. 26.
    For more details, see, for example, D. Voet, J.G. Voet, and C.W. Pratt, Fundamentals of Biochemistry. John Wiley & Sons, New York, 1999, pp. 492–528.Google Scholar
  21. 28.
    D.W. Urry, L.C. Hayes, and D. Channe Gowda, “Electromechanical Transduction: Reduction-driven Hydrophobic Folding Demonstrated in a Model Protein to Perform Mechanical Work.” Biochem. Biophys. Res. Commun., 204, 230–237, 1994.PubMedCrossRefGoogle Scholar
  22. 29.
    A. Pattanaik, D. Channe Gowda, and D.W. Urry, “Phosphorylation and Dephosphorylation Modulation of an Inverse Temperature Transition.” Biochem. Biophys. Res. Commun., 178, 539–545, 1991.PubMedCrossRefGoogle Scholar
  23. 30.
    D.W. Urry, D. Channe Gowda, S.Q. Peng, and T.M. Parker, “Non-linear Hydrophobic-induced pKa Shifts: Implications for Efficiency of Conversion to Chemical Energy.” Chem. Phys. Lett., 239, 67–74, 1995. A millionfold increase in affinity is what would be required for pumping protons into the stomach.CrossRefGoogle Scholar
  24. 31.
    D.W. Urry, L.C. Hayes, D. Channe Gowda, S.Q. Peng, and N. Jing, “Electrochemical Transduction in Elastic Protein-based Polymers.” Biochem. Biophys. Res. Commun., 210, 1031–1039, 1995.PubMedCrossRefGoogle Scholar
  25. 32.
    For more general details, see, for example, D. Voet, J.G. Voet, and C.W. Pratt, Fundamentals of Biochemistry. John Wiley & Sons, New York, 1999, pp. 180–186. Muscle contraction is also treated in some detail in Chapter 8.Google Scholar
  26. 33.
    P. Mitchell, “Keilin’s Respiratory Chain Concept and its Chemiosmotic Consequences.” Science, 206, 1148–1159, 1979.PubMedCrossRefGoogle Scholar
  27. 34.
    I.Z. Steinberg, A. Oplatka, and A Katchalsky, “Mechanochemical Engines.” Nature, 210, 568–571, 1966.CrossRefGoogle Scholar
  28. 36.
    D.W. Urry, “Free Energy Transduction in Polypeptides and Proteins Based on Inverse Temperature Transitions.” Prog. Biophys. Mol. Biol., 57, 23–57, 1992.PubMedCrossRefGoogle Scholar
  29. 37.
    D.M. Himmel, S. Gourinath, L. Reshetnikova, Y. Shen, A.G. Szent-Györgyi, and C. Cohen, “Crystallographic Findings on the Internally Uncoupled and Near Rigor States of Myosin: Further Insights into the Mechanics of the Motor.” Proc. Natl. Acad. Sci. U.S.A., 99, 12645–12650, 2002.PubMedCrossRefGoogle Scholar
  30. 39.
    A.R. Fersht, “The Charging of tRNA.” In Accuracy in Molecular Processes: Its Control and Relevance to Living Systems, T.B.L. Kirkwood, R.F. Rosenberger, and D.J. Galas, Eds., Chapman and Hall, London, 1986, pp. 67–82.Google Scholar
  31. 40.
    D.W. Urry and H. Eyring, “Stereochemistry and Rate Theory in Protein Synthesis.” Arch. Biochem. Biophys., Suppl. 1, 52–62, 1962.Google Scholar
  32. 41.
    J. Bronowski, The Ascent of Man. Little, Brown and Company, Boston/Toronto, 1973, p. 110.Google Scholar
  33. 42.
    D.T. McPherson, J. Xu, and D.W. Urry, “Product Purification by Reversible Phase Transition Following E. coli Expression of Genes Encoding up to 251 Repeats of the Elastomeric Pentapeptide GVGVP.” Protein Expression Purification, 7, 51–57, 1996.PubMedCrossRefGoogle Scholar
  34. 43.
    D.W. Urry, D.T. McPherson, J. Xu, H. Daniell, C. Guda, D.C. Gowda, N. Jing, T.M. Parker, “Proteinbased Polymeric Materials: Syntheses and Properties.” In The Polymeric Materials Encyclopedia: Synthesis, Properties and Applications, CRC Press, Boca Raton, pp. 7263–7279, 1996.Google Scholar
  35. 44.
    D.W. Urry and A. Pattanaik, “Elastic Proteinbased Materials in Tissue Reconstruction.” Ann. N.Y. Acad. Sci., 831, 32–46, 1997.PubMedCrossRefGoogle Scholar
  36. 45.
    D.W. Urry, “Engineers of Creation.” Chemistry in Britain, 32, 39–42, 1996.Google Scholar
  37. 46.
    Dan W. Urry, “Elastic Molecular Machines in Metabolism and Soft Tissue Restoration.” TIBTECH, 17, 249–257 (1999).Google Scholar
  38. 47.
    N. Wang, J.P. Butler, and D.E. Ingber, “Mechanotransduction across the cell surface and through the cytoskeleton.” Science, 260, 1124–1127, 1993.PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media, LLC 2006

Personalised recommendations