Consilient Mechanisms for Diverse Protein-based Machines: The Efficient Comprehensive Hydrophobic Effect


The machines of biology are of a mechanism more elemental than those of man’s design. Consider, for example, the intermittent internal combustion (e.g., gasoline-reciprocating piston) engine that performs the work of putting a vehicle in motion. Fuel is injected in a timely manner into a series of chambers; the fuel vapors are ignited in each chamber; a series of explosions of hot expanding gasses occur in properly timed sequence; the hot expanding gasses supply the energy that drives the pistons, that by means of connecting rods rotates the crankshaft, that through a clutch assembly and speed-changing gears rotates the drive shaft, that by means of a differential gear box rotates the wheels, that puts the vehicle in motion.


Gibbs Free Energy Model Protein Mechanical Work Elastic Band Molecular Machine 
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.
    E.O. Wilson, Consilience, The Unity of Knowledge. Alfred E. Knopf, New York, 1998, page 8, gives a definition of the word consilience as providing a “common groundwork of explanation.”Google Scholar
  2. 3.
    E.O. Wilson, Consilience: The Unity of Knowledge. Alfred E. Knopf, New York, 1998, pp. 4–5.Google Scholar
  3. 4.
    D.W. Urry, “Physical Chemistry of Biological Free Energy Transduction as Demonstrated by Elastic Protein-based Polymers.” J. Phys. Chem. B, 101, 11007–11028, 1997.Google Scholar
  4. 5.
    Concepts Introduced During Development of Elastic Protein-based Polymers for Free Energy Transduction: The conclusions of this article can also be given in terms of the following chronological listing of the concepts introduced during the development of elastic protein-based polymers for free energy transduction: (1) the concept of the damping of internal chain dynamics on extension as the source of entropic elastomeric force, called the librational entropy mechanism of elasticity; (2) the concept of T t, the temperature of the hydrophobic folding and assembly transition, being used as the fundamental measure of hydrophobicity and providing a practical on-off switching capacity; (3) the generally obvious concept that raising the temperature from below to above T t is a means of performing mechanical work by cross-linked elastic protein-based polymers; (4) the concept of the ΔT t-mechanism wherein the value of T t is changed, rather than the temperature, as a means of achieving free energy transduction; (5) the concept of energy conversion by means of the coupling of different functional moieties by being part of the same hydrophobic folding and assembly domain arising out of, for example, (a) hydrophobic-induced pKa shifts, (b) hydrophobic-induced shift in redox potential, and (c) demonstrated coupling of carboxyl and redox functions to result in electrochemical transduction; (6) the concept of the competition for hydration between apolar (hydrophobic) and polar (e.g., charged) moieties to give rise to pKa shifts and positive cooperativity; (7) the concept of ‘poising’ for achieving higher efficiencies; (8) essential equivalence of the inverse temperature transition of a phase separation and the intramolecular phase separation of the hydrophobic folding of a globular protein or assembly of the protomer subunits to form a multisubunit globular protein such as phosphofructose kinase, that is, the extension to globular proteins; and (9) extension to all polymers where, however, the degree of expression of the above effects is limited due to the lack of the many advantages of protein-based polymers of Table I.” (From Urry.) 4CrossRefGoogle 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, “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
  7. 8.
    D.W. Urry, “The Change in Gibbs Free Energy for Hydrophobic Association: Derivation and Evaluation by means of Inverse Temperature Transitions”. Chem. Phys. Letters, 399, 177–183, 2004.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, issue 5–6 (2002); Special Issue: Mechanics of Elastic Biomolecules, H. Granzier, M. Kellermayer, W. Linke, Eds.Google Scholar
  9. 15.
    F. Franks, “Protein Destabilization at Low Temperatures.” Adv. Protein Chem., 46, 107–139, 1995.Google Scholar
  10. 16.
    P.L. Privalov, “Cold Inactivation of Enzymes.” Crit. Rev. Biochem. Mol. Biol., 25, 281–305, 1990.PubMedCrossRefGoogle Scholar
  11. 17.
    The term inverse transition was first used in connection with the increase in order of the antibiotic stendomycin on raising the temperature (D.W. Urry and A. Ruiter, “Conformation of Polypeptide Antibiotics. VI. Circular Dichroism of Stendomycin.” Biochem. Biophys. Res. Commun., 38, 800–806, 1970). The term became specifically inverse temperature transition in relation to coacervation of elastin fragments that exhibited a phase separation with increased order on raising the temperature (B.C. Starcher, G. Saccomani, and D.W. Urry, “Coacervation and Ion-Binding Studies on Aortic Elastin.” Biochim. Biophys. Acta, 310, 481–486, 1973, and D.W. Urry, B. Starcher, and S.M. Partridge, “Coacervation of Solubilized Elastin Effects a Notable Conformational Change”. Nature, 222, 795–796, 1969).PubMedCrossRefGoogle Scholar
  12. 18.
    P.J. Flory, Principles of Polymer Chemistry. Cornell University Press, Ithaca, New York, 1953, Figure 121.Google Scholar
  13. 19.
    M. Manno, A. Emanuele, V. Martorana, P.L. San Biagio, D. Bulone, M.B. Palma-Vitorelli, D.T. McPherson, J. Xu, T.M. Parker, and D.W. Urry, “Interaction of Processes on Different/time scales in a bioelastomer capable of performing energy conversion.” Biopolymers, 59, 51–64, 2001.PubMedCrossRefGoogle Scholar
  14. 20.
    F. Sciortino, K.U. Prasad, D.W. Urry, and M.U. Palma, “Self-Assembly of Bioelastomeric Structures From Solutions: Mean Field Critical Behavior and Flory-Huggins Free-Energy of Interaction.” Biopolymers, 33, 743–52, 1993.PubMedCrossRefGoogle Scholar
  15. 21.
    B.A. Cox, B.C. Starcher, and D.W. Urry, “Coacervation of α-Elastin Results in Fiber Formation.” Biochim. Biophys. Acta., 317, 209–213, 1973.PubMedGoogle Scholar
  16. 22.
    B.A. Cox, B.C. Starcher, and D.W. Urry, “Coacervation of Tropoelastin Results in Fiber Formation.” J. Biol. Chem., 249, 997–998, 1974.PubMedGoogle Scholar
  17. 23.
    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
  18. 24.
    W.J. Cook, H.M. Einspahr, T.L. Trapane, D.W. Urry, and C.E. Bugg, “Crystal Structure and Conformation of the Cyclic Trimer of a Repeat Pentapeptide of Elastin, Cyclo-(L-Valyl-L-prolylglycyl-L-valyglycyl)3.” J. Am. Chem. Soc., 102, 5502–5505, 1980.CrossRefGoogle Scholar
  19. 25.
    J.A.V. Butler, “The energy and entropy of hydration of organic compounds.” Transaction Faraday Society, 33, 229–238, 1937.CrossRefGoogle Scholar
  20. 26.
    H.S. Frank and M.E. Evans, “Free Volume and Entropy in Condensed Systems: III. Entropy in Binary Liquid Mixtures; Partial Molal Entropy in Dilute Solutions; Structure and Thermodynamics in Aqueous Electrolytes.” J. Chem. Phys., 13, 507–532, 1945.CrossRefGoogle Scholar
  21. 28.
    D.W. Urry, T.L. Trapane, and K.U. Prasad, “Phase-Structure Transitions of the Elastin Polypentapeptide-Water System Within the Framework of Composition-Temperature Studies.” Biopolymers, 24, 2345–2356, 1985.PubMedCrossRefGoogle Scholar
  22. 29.
    D.W. Urry, D.T. McPherson, J. Xu, H. Daniell, C. Guda, D.C. Gowda, N. Jing, and T.M. Parker, “Protein-Based Polymeric Materials: Syntheses and Properties.” In The Polymeric Materials Encyclopedia: Synthesis, Properties and Applications, CRC Press, Boca Raton, pp. 7263–7279, 1996. See Figure 6.Google Scholar
  23. 31.
    F. Sciortino, M.U. Palma, D.W. Urry, and K.U. Prasad, “Nucleation and Accretion of Bioelastomeric Fibers at Biological Temperatures and Low Concentrations.” Biochem. Biophys. Res. Commun. 157, 1061–1066, 1988.PubMedCrossRefGoogle Scholar
  24. 35.
    D.W. Urry, S-Q. Peng, J. Xu, and D.T. McPherson, “Characterization of Waters of Hydrophobic Hydration by Microwave Dielectric Relaxation.” J. Amer. Chem. Soc., 119, 1161–1162, 1997.CrossRefGoogle Scholar
  25. 40.
    D.W. Urry, D.C. 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.CrossRefGoogle Scholar
  26. 41.
    D.W. Urry, S.Q. Peng, L.C. Hayes, D.T. McPherson, Jie Xu, T.C. Woods, D.C. Gowda, and A. Pattanaik, “Engineering Protein-based Machines to Emulate Key Steps of Metabolism (Biological Energy Conversion).” Biotechnol. Bioeng., 58, 175–190, 1998.PubMedCrossRefGoogle Scholar
  27. 42.
    D.W. Urry, L. Hayes, C.X. Luan, D.C. Gowda, D. McPherson, J. Xu, and T. Parker, “ΔT t-Mechanism in the Design of Self-Assembling Structures,” In Self-assembling Peptide Systems in Biology, Medicine and Engineering. A. Aggeli, N. Boden, S. Zhang, Eds., Kluwer Academic Publishers, Dordrecht, The Netherlands, 2001, pp. 323–340.Google Scholar
  28. 44.
    D.W. Urry and M.M. Long, “Conformations of the Repeat Peptides of Elastin in Solution: An Application of Proton and Carbon-13 Magnetic Resonance to the Determination of Polypeptide Secondary Structure.” CRC Crit. Rev. Biochemistry, 4, 1–45, 1976.CrossRefGoogle Scholar
  29. 45.
    D.W. Urry, “Characterization of Soluble Peptides of Elastin by Physical Techniques.” In Methods in Enzymology, 82, 673–716, 1982. (L.W. Cunningham and D.W. Frederiksen, Eds.) Academic Press, Inc., New York, New York.Google Scholar
  30. 46.
    D.W. Urry, C.M. Venkatachalam, M.M. Long, and K.U. Prasad, “Dynamic β-Spirals and A Librational Entropy Mechanism of Elasticity.” In Conformation in Biol. (R. Srinivasan and R.H. Sarma, Eds.) G.N. Ramachandran Festschrift Volume, Adenine Press, USA, 11–27, 1982.Google Scholar
  31. 47.
    D.W. Urry, “Thermally Driven Self-assembly, Molecular Structuring and Entropic Mechanisms in Elastomeric Polypeptides.” In Mol. Conformation and Biol. Interactions (P. Balaram and S. Ramaseshan, Eds.) Indian Acad. of Sci., Bangalore, India, pp. 555–583, 1991.Google Scholar
  32. 48.
    D.W. Urry, T. Hugel, M. Seitz, H. Gaub, L. Sheiba, J. Dea, J. Xu, and T. Parker, “Elastin: A Representative Ideal Protein Elastomer.” Phil. Trans. R. Soc. Lond., B 357, 169–184, 2002.CrossRefGoogle Scholar
  33. 49.
    D.W. Urry, T. Hugel, M. Seitz, H. Gaub, L. Sheiba, J. Dea, J. Xu, L. Hayes, F. Prochazka, and T. Parker, In Ideal Protein Elasticity: The Elastin Model, P. Shewry and A. Bailey, Eds., Cambridge University Press, (in press) 2003.Google Scholar
  34. 50.
    L.B. Sandberg, J.G. Leslie, C.T. Leach, V.L. Torres, A.R. Smith, and D.W. Smith, “Elastin Covalent Structure as Determined by Solid State Amino Acid Sequencing.” Pathol. Biol., 33, 266–274, 1985.PubMedGoogle Scholar
  35. 51.
    H. Yeh, N. Ornstein-Goldstein, Z. Indik, P. Sheppard, N. Anderson, J.C. Rosenbloom, G. Cicila, K. Yoon, and J. Rosenbloom, “Sequence Variation of Bovine Elastin mRNA due to Alternative Splicing.” J. Collagen Rel. Res., 7, 235–247, 1987.Google Scholar
  36. 53.
    G.J. Thomas, Jr., B. Prescott, and D.W. Urry, “Raman Amide Bands of Type-II β-Turns in Cyclo-(VPGVG)3 and Poly(VPGVG), and Implications for Protein Secondary Structure Analysis.” Biopolymers, 26, 921–934, 1987.PubMedCrossRefGoogle Scholar
  37. 54.
    D. Volpin, D.W. Urry, I. Pasquali-Ronchetti, and L. Gotte, “Studies by Electron Microscopy on the Structure of Coacervates of Synthetic Polypeptides of Tropoelastin.” Micron, 7, 193–198, 1976.Google Scholar
  38. 55.
    D.W. Urry, C.M. Venkatachalam, M.M. Long, and K.U. Prasad, “Dynamic β-Spirals and a Librational Entropy Mechanism of Elasticity.” In Conformation in Biology, R. Srinivasan and R.H. Sarma, Eds., G.N. Ramachandran Festschrift Volume, Adenine Press, USA, 11–27, 1982.Google Scholar
  39. 56.
    D.K. Chang and D.W. Urry, “Polypentapeptide of Elastin: Damping of Internal Chain Dynamics on Extension.” J. Computational Chem., 10, 850–855, 1989.CrossRefGoogle Scholar
  40. 57.
    T. Hugel, M. Seitz, H. Gaub, and D. Urry, unpublished results.Google Scholar
  41. 58.
    C.A.J. Hoeve and P.J. Flory “Elastic Properties of Elastin.” Biopolymers, 13, 677–686, 1974.PubMedCrossRefGoogle Scholar
  42. 59.
    T. Weis-Fogh and S.O. Andersen, “New Molecular Model for the Long-range Elasticity of Elastin.” Nature, 227, 718–721, 1970.PubMedCrossRefGoogle Scholar
  43. 60.
    L.B. Alonso, B.J. Bennion, and V. Daggett, “Hydrophobic Hydration is an Important Source of Elasticity in Elastin-based Polymers.” J. Am. Chem. Soc., 123, 11991–11998, 2001.PubMedCrossRefGoogle Scholar
  44. 61.
    Z.R. Wasserman and F.R. Salemme, “A Molecular Dynamics Investigation of the Elastomeric Restoring Force in Elastin.” Biopolymers, 29, 1613–1631, 1990.PubMedCrossRefGoogle Scholar
  45. 62.
    P. J. Flory, “Molecular Interpretation of Rubber Elasticity.” Rubber Chem. Tech., 41, G41–G48, 1968.Google Scholar
  46. 63.
    C.-H. Luan, J. Jaggard, R.D. Harris, and D.W. Urry, “On the Source of Entropic Elastomeric Force in Polypeptides and Proteins: Backbone Configurational vs. Side Chain Solvational Entropy.” Int. J. Quant. Chem. Quant. Biol. Symp., 16, 235–244, 1989.Google Scholar
  47. 64.
    D.W. Urry, B. Haynes, H. Zhang, R.D. Harris, and K.U. Prasad, “Mechanochemical Coupling in Synthetic Polypeptides by Modulation of an Inverse Temperature Transition.” Proc. Natl. Acad. Sci. USA, 85, 3407–3411, 1988.PubMedCrossRefGoogle Scholar
  48. 65.
    D.W. Urry, “Protein Folding and Assembly: An Hydration-Mediated Free Energy Driving Force.” In Protein Folding: Deciphering the Second Half of the Genetic Code. (Lila Gierasch and Johanathan King, Eds.), Am. Assoc. for the Advancement of Sci., Washington, D. C., 63–71, 1990.Google Scholar
  49. 66.
    D.W. Urry, J. Xu, W. Wang, L. Hayes, F. Prochazka, and T.M. Parker, “Development of Elastic Protein-based Polymers as Materials for Acoustic Absorption.” Mat. Res. Soc. Symp. Proc.: Materials Inspired by Biology, 774, 81–92, 2003.Google Scholar
  50. 67.
    D.W. Urry, T.C. Woods, L.C. Hayes, J. Xu, D.T. McPherson, M. Iwama, M. Furuta, T. Hayashi, M. Murata, and T. M. Parker, “Elastic Protein-Based Biomaterials: Elements of Basic Science, Controlled Release and Biocompatibility.” In: Tissue Engineering and Novel Delivery Systems, Marcel Dekker, Inc. New York, Chapter 2, pp. 31–54, 2004.Google Scholar
  51. 68.
    As reported in L.P. Wheeler, Josiah Willard Gibbs, the History of a Great Mind; Yale University Press: New Haven, CT, and London, 1952; pp 88–89, this statement was penned by J. Willard Gibbs in an 1881 letter to the American Academy of Arts and Sciences.Google Scholar
  52. 71.
    C.J. Heimbach, Photochemical Transduction by Hydrophobically Poised Bioelastic Proteins. Ph.D. Dissertation, The University of Alabama, Birmingham, 1998.Google Scholar
  53. 72.
    C.-H. Luan and D.W. Urry, “Elastic, Plastic, and Hydrogel Protein-based Polymers.” In Polymer Data Handbook, J.E. Mark, Ed., 1999, Oxford University Press, New York, pp. 78–89, Tables 1 and 3a.Google Scholar
  54. 73.
    D.W. Urry, L.C. Hayes, D.C. Gowda, S.-Q. Peng, and N. Jing, “Electro-chemical Transduction in Elastic Protein-based Polymers.” Biochem. Biophys. Res. Commun., 210, 1031–1039, 1995.PubMedCrossRefGoogle Scholar
  55. 74.
    A. Pattanaik, D.C. Gowda, and D.W. Urry, “Phosphorylation and Dephosphorylation Modulation of an Inverse Temperature Transition.” Biochem. Biophys. Res. Comm., 178, 539–545, 1991.PubMedCrossRefGoogle Scholar
  56. 76.
    C.-H. Luan, T. Parker, K.U. Prasad, and D.W. Urry, “DSC Studies of NaCl Effect on the Inverse Temperature Transition of Some Elastin-based Polytetra-, Polypenta-, and Polynonapeptides.” Biopolymers, 31, 465–475, 1991.PubMedCrossRefGoogle Scholar
  57. 77.
    D.W. Urry, M.M. Long, R.D. Harris, and K.U. Prasad, “Temperature Correlated Force and Structure Development in Elastomeric Polypeptides: The Ile1 Analog of the Polypentapeptide of Elastin.” Biopolymers, 25, 1939–1953, 1986.PubMedCrossRefGoogle Scholar
  58. 78.
    D.W. Urry, R.D. Harris, M.M. Long, and K.U. Prasad, “Polytetrapeptide of Elastin: Temperature Correlated Elastomeric Force and Structure Development” Int. J. Pept. Protein Res., 28, 649–660, 1986.PubMedCrossRefGoogle Scholar
  59. 79.
    D.W. Urry, R.D. Harris, and K.U. Prasad, “Chemical Potential Driven Contraction and Relaxation by Ionic Strength Modulation of an Inverse Temperature Transition.” J. Am. Chem. Soc., 110, 3303–3305, 1988.CrossRefGoogle Scholar
  60. 80.
    D.W. Urry, L.C. Hayes, T.M. Parker, and R.D. Harris, “Baromechanical Transduction in a Model Protein by the ΔTt Mechanism.” Chem. Phys. Lett., 201, 336–340, 1993.CrossRefGoogle Scholar
  61. 81.
    D.W. Urry, L.C. Hayes, and D.C. 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
  62. 82.
    D. W. Urry, “Engineers of Creation.” Chemistry in Britain, 39–42, 1996.Google Scholar
  63. 83.
    D.W. Urry, L.C. Hayes, D.C. Gowda, C.M. Harris, and R.D. Harris, “Reduction-driven Polypeptide Folding by the ΔTt Mechanism.” Biochem. Biophys. Res. Commun., 188, 611–617, 1992.PubMedCrossRefGoogle Scholar
  64. 84.
    D.W. Urry, L.C. Hayes, D.C. Gowda, and T.M. Parker, “Pressure Effect on Inverse Temperature Transitions: Biological Implications.” Chem. Phys. Lett., 182, 101–106, 1991.CrossRefGoogle Scholar
  65. 85.
    L.A. Strzegowski, M.B. Martinez, D.C. Gowda, D.W. Urry, and D.A. Tirrell, “Photomodulation of the Inverse Temperature Transition of a Modified Elastin Poly(pentapeptide).” J. Am. Chem. Soc., 116, 813–814, 1994.CrossRefGoogle Scholar
  66. 86.
    D.W. Urry, S.-Q. Peng, L. Hayes, J. Jaggard, and R.D. Harris, “A New Mechanism of Mechanochemical Coupling: Stretch-induced Increase in Carboxyl pKa as a Diagnostic.” Biopolymers, 30, 215–218, 1990.PubMedCrossRefGoogle Scholar
  67. 87.
    D.W. Urry and S.-Q. Peng, “Non-linear Mechanical Force-induced pKa Shifts: Implications for Efficiency of Conversion to Chemical Energy.” J. Am. Chem. Soc., 117, 8478–8479, 1995.CrossRefGoogle Scholar
  68. 88.
    R. Henze and D.W. Urry, “Dielectric Relaxation Studies Demonstrate a Peptide Librational Mode in the Polypentapeptide of Elastin.” J. Am. Chem. Soc., 107, 2991–2993, 1985.CrossRefGoogle Scholar
  69. 89.
    R. Buchet, C.-H. Luan, K.U. Prasad, R.D. Harris, and D.W. Urry, “Dielectric Relaxation Studies on Analogs of the Polypentapeptide of Elastin.” J. Phys. Chem., 92, 511–517, 1988.CrossRefGoogle Scholar
  70. 90.
    I.Z. Steinberg, A. Oplatka, and A. Katchalsky, “Mechanochemical Engines.” Nature, 210, 568–571, 1966.CrossRefGoogle Scholar
  71. 91.
    M.V. Stackelberg and H.R. Müller, “Zur Struktur der Gashydrate.” Naturwissenschaften, 38, 456, 1951; M.V. Stackelberg and H.R. Müller, “Feste Gashydrate II: Struktur und Raumchemie.” Z. Elektochem., 54, 25–39, 1954.CrossRefGoogle Scholar
  72. 92.
    M.M. Teeter, “Hydrophobic Protein at Atomic Resolution: Pentagonal Rings of Water Molecules in Crystals of Crambin.” Proc. Natl. Acad. Sci. U.S.A., 81, 6014–6018, 1984.PubMedCrossRefGoogle Scholar
  73. 93.
    D.W. Urry, S.-Q. Peng, and T.M. Parker, “Delineation of Electrostatic-and Hydrophobic-Induced pKa Shifts in Polypentapeptides: The Glutamic Acid Residue.” J. Am. Chem. Soc., 115, 7509–7510, 1993.CrossRefGoogle Scholar
  74. 94.
    D.W. Urry, C.-H. Luan, R.D. Harris, and K.U. Prasad, “Aqueous Interfacial Driving Forces in the Folding and Assembly of Protein (Elastin)-Based Polymers: Differential Scanning Calorimetry Studies.” Polym. Preprints, Div. Polym. Chem., Am. Chem. Soc., 31, 188–189, 1990.Google Scholar
  75. 95.
    A. Katchalsky, S. Lifson, I. Michaeli, and M. Zwick, “Elementary Mechanochemical Processes.” In Size & Shape of Contractile Polymers: Conversion of Chemical & Mechanical Energy. Pergamon Press, New York, 1960, pp. 1–40, see page 11.Google Scholar
  76. 96.
    J. Wyman, “Allosteric Effects in Hemoglobin.” Cold Spring Harbor Symp. Quant. Biol., 28, 483–489, 1963.Google Scholar
  77. 97.
    A.V. Hill, “The Possible Effect of the Aggregation of Hemoglobin on its Dissociation Curves.” Proceedings of the Physiological Society, J. Physiol., 40, iv–vii, 1910, and A.V. Hill J. Biochem., 7, 471–480, 1913.Google Scholar
  78. 98.
    D.W. Urry, S.-Q. Peng, D.C. Gowda, T.M. Parker, and R.D. Harris, “Comparison of Electrostatic-and Hydrophobic-induced pKa Shifts in Polypentapeptides: The Lysine Residue.” Chem. Phys. Lett., 225, 97–103, 1994.CrossRefGoogle Scholar
  79. 99.
    D.W. Urry, S.-Q. Peng, T.M. Parker, D.C. Gowda, and R.D. Harris, “Relative Significance of Electrostatic-and Hydrophobic-Induced pKa Shifts in a Model Protein: The Aspartic Acid Residue.” Angew. Chem. [German], 105, 1523–1525, 1993; Angew. Chem. Int. Ed. Engl., 32, 1440–1442, 1993.CrossRefGoogle Scholar
  80. 100.
    D.W. Urry, D.C. Gowda, S.-Q. Peng, T.M. Parker, N. Jing, and R.D. Harris, “Nanometric Design of Extraordinary Hydrophobicity-induced pKa Shifts for Aspartic Acid: Relevance to Protein Mechanisms.” Biopolymers, 34, 889–896, 1994, Figures 4 and 5B.PubMedCrossRefGoogle Scholar
  81. 101.
    D.W. Urry, D.T. McPherson, J. Xu, H. Daniell, C. Guda, D.C. Gowda, N. Jing, and T.M. Parker, “Protein-based Polymeric Materials: Syntheses and Properties.” In The Polymeric Materials Encyclopedia: Synthesis, Properties and Applications. CRC Press, Boca Raton, FL, pp. 7263–7279, 1996.Google Scholar
  82. 102.
    T. Cooper Woods, Protein-based polymers as Delivery Vehicles for Antisense Oligonucleotides. Ph.D. Dissertation, University of Alabama, Birmingham, 1998.Google Scholar
  83. 103.
    L. Hayes, Effect of Hydrophobicity of Elastic Protein-based Polymers on Redox Potential. Ph.D. Dissertation, University of Alabama, Birmingham, 1998.Google Scholar
  84. 104.
    M.F. Perutz, “Mechabnisms of Cooperativity and Allosteric Regulation in Proteins.” Q. Rev. Biophys., 22, 139–236, 1989.PubMedCrossRefGoogle Scholar
  85. 106.
    C. Bohr, K.A. Hasselbalch, and A. Krogh, “Uber einem in biologischen Beziehung wichtigen Einfluss, den die Kohlensaurenspannung des Blutes auf dessen Sauerstoffbinding übt.” Skand. Arch. Physiol., 16, 401–412, 1904.Google Scholar
  86. 107.
    G. S. Adair, “The Hemoglobin System. VI. The Oxygen Dissociation Curve of Hemoglobin.” J. Biol. Chem., 63, 529–545, 1925.Google Scholar
  87. 108.
    J. Monod, J.-P. Changeux, and F. Jacob, “Allosteric proteins and molecular control systems.” J. Mol. Biol., 6, 306–329, 1963.PubMedCrossRefGoogle Scholar
  88. 109.
    J. Monod, J. Wyman, and J.-P. Changeux, “On the nature of allosteric transitions: a plausible model.” J. Mol. Biol., 12, 88–118, 1965.PubMedCrossRefGoogle Scholar
  89. 110.
    D.E. Koshland, G. Nemethy, and D. Filmer, “Comparison of experimental binding data and theoretical models in proteins containing subunits.” Biochemistry, 5, 365–385, 1966.PubMedCrossRefGoogle Scholar
  90. 111.
    J. Monod, “On Symmetry and Function in Biological Systems.” In Nobel Symposium 11: Symmetry and Function of Biological Systems at the Macromolecular Level. (A. Engstrom and B. Strandberg, eds.), Almqvist & Wiksell Forlag AB, Stockholm, 1968, page 1527. Also reprinted in Selected Papers in Molecular Biology by Jacques Monod, A. Lwoff and A. Ullmann, Eds Academic Press, 1978, page 708.Google Scholar
  91. 112.
    G. Weber, Protein Interactions. Chapman and Hall, New York, 1992, page 104.Google Scholar
  92. 113.
    A. Katchalsky, “Solutions of Polyelectrolytes and Mechanochemical Systems.” J. Polymer Sci., 7, 393–412, 1951.CrossRefGoogle Scholar
  93. 115.
    F.E. Harris and S.A. Rice, “A Chain Model of Polyelectrolytes. I.” J. Phys. Chem., 581, 725–732, 1954.CrossRefGoogle Scholar
  94. 116.
    J.Th.G. Overbeek, “The Dissociation and Titration Constants of Polybasic Acids.” Bull. Soc. Chim. Belg., 57, 252–261, 1948.CrossRefGoogle Scholar
  95. 117.
    C.-H. Luan, T. Parker, K.U. Prasad, and D.W. Urry, “DSC Studies of NaCl Effect on the Inverse Temperature Transition of Some Elastin-based Polytetra-, Polypenta-, and Polynonapeptides.” Biopolymers, 31, 465–475, 1991.PubMedCrossRefGoogle Scholar
  96. 118.
    H. S. Harned and B. B. Owen, The Physical Chemistry of Electrolyte Solutions. 3rd Ed. Rheinhold, New York, 1967.Google Scholar
  97. 119.
    D.W. Urry, “What is Elastin; What is Not.” Ultrastruct. Pathol., 4, 227–251, 1983.PubMedCrossRefGoogle Scholar
  98. 120.
    D.W. Urry, K. Okamoto, R.D. Harris, C.F. Hendrix, and M.M. Long, “Synthetic, Cross-Linked Polypentapeptide of Tropoelastin: An Anisotropic, Fibrillar Elastomer.” Biochemistry, 15, 4083–4089, 1976.PubMedCrossRefGoogle Scholar
  99. 121.
    D. W. Urry, “Free Energy Transduction in Polypeptides and Proteins Based on Inverse Temperature Transition.” Prog. Biophys. Molec. Biol., 57, 23–57, 1992.CrossRefGoogle Scholar
  100. 122.
    D. W. Urry, “Five Axioms for the Functional Design of Peptide-Based Polymers as Molecular Machines and Materials: Principle for Macromolecular Assemblies.” Biopolymers (Peptide Science), 47, 167–178 (1998).CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media, LLC 2006

Personalised recommendations