Determining temperature-invariant enthalpy change and other thermodynamic functions on transformation of proteins and other biopolymers

Journal of Physical Chemistry B

Volumn 101, Issue 34, 1997, Pages 6780-6785

  Johari, G P ^a  

^a MCMASTER UNIVERSITY   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

BIOPOLYMERS; CALCULATIONS; DEGREES OF FREEDOM (MECHANICS); ENTHALPY; ENTROPY; MATHEMATICAL MODELS; MOLECULES; PHASE TRANSITIONS; THERMODYNAMICS;

BENZINGER METHOD; ENTHALPY CHANGE;

PROTEINS;

EID: 0031213481     PISSN: 15206106     EISSN: None     Source Type: Journal    
DOI: 10.1021/jp9708613     Document Type: Article

References (56)

1. Treptow, R. S. J. Chem. Educ. 1995, 72, 497.
2. Benzinger. T. H. Nature (London) 1971, 229, 100.
3. Planck, M. Treatise on Thermodynamics, 3rd ed.; Dover: New York, 1965 (translated by Alexander Ogg from the 7th German ed.).
4. exc carries the immediate meaning that at the temperature concerned, the changes are irreversible, as is the case at all temperatures other than that at thermodynamic equilibrium.
5. exc carries the immediate meaning that at the temperature concerned, the changes are irreversible, as is the case at all temperatures other than that at thermodynamic equilibrium.
6. Chun, P. W. J. Phys. Chem. 1994, 98, 6851; Ibid. 1996, 100, 7283 and references cited therein; J. Biol. Chem. 1995, 13925.
7. Chun, P. W. J. Phys. Chem. 1994, 98, 6851; Ibid. 1996, 100, 7283 and references cited therein; J. Biol. Chem. 1995, 13925.
8. Chun, P. W. J. Phys. Chem. 1994, 98, 6851; Ibid. 1996, 100, 7283 and references cited therein; J. Biol. Chem. 1995, 13925.
9. Stryer, L. Biochemistry: Freeman: San Francisco, 1988.
10. Privalov, P. L. Annu. Rev. Biophys. Biophys. Chem. 1989, 18, 47.
11. Frauenfelder, H.; Nienhaus, G. U.; Young, R. D. Relaxation and Disorder in Proteins. In Disorder Effects in Relaxational Processes; Richert, R., Blumen, A., Eds.; Springer Verlag: Berlin, 1994; p 591.
12. Frauenfelder, H.; Parak, F.; Young, R. D. Annu. Rev. Biophys. Biophys. Chem. 1988, 17, 451.
13. Doster, W.; Post, F.; Settles. M. Origin of Non-Exponential Relaxations in Proteins. In Disorder Effects in Relaxational Processes; Richert, R., Blumen, A., Eds.; Springer Verlag: Berlin, 1994: p 615.
14. Stein, D. L. Proc. Natl. Acad. Sci. U.S.A. 1985, 82, 3670.
15. Gregory, R. B. In Protein-Solvent Interactions; Gregory, R. B., Ed.; Marcel-Dekker, Inc: New York, 1995; p 191 and references cited therein.
16. Sartor, G.; Hallbrucker, A.; Hofer, K; Mayer, E. J. Phys. Chem. 1992, 96, 5133.
17. Sartor, G.; Mayer, E.; Johari, G. P. Biophys. J. 1994, 66, 249.
18. Green, J. L.; Fan, J.; Angell, C. A. J. Phys. Chem. 1994, 98, 13780.
19. Sartor, G.; Johari, G. P. J. Phys. Chem. 1996, 100, 10450.
20. Johari, G. P.; Sartor, G. J. Chem. Soc., Faraday Trans. 1996, 22, 4521.
21. Sartor, G.; Johari, G. P. J. Phys. Chem. 1996, 100, 19692.
22. Ruedisser, S.; Hallbrucker, A; Mayer, E. J. Phys. Chem. 1996, 100, 458.
23. Frauenfelder, H.; Pretsko, G. A.; Tsenoglou, D. Nature (London) 1979, 280, 558.
24. Aitymiuk, P. J.; Blake, C. C. F.; Grace, D. E. P.; Oatley, S. J.; Philips, D. C.; Stemberg, M. J. E. Nature (London) 1979, 280, 563.
25. Hartman, H.; Parak, F.; Steigemann, W.; Petsko, G. A.; Ringe Ponze, D.; Frauenfelder, H. Proc. Natl. Acad. Sci. U.S.A. 1982, 79, 4967.
26. Petsko, G. A.; Ringe, D. Annu. Rev. Biophys. Biophys. Chem. 1984, 13, 331.
27. Keller, H.; Debrunner, P. G. Phys. Rev. Lett. 1980, 45, 68.
28. Parak, F.; Knapp, E. W.; Kucheida, D. J. Mol. Biol. 1982, 161, 177.
29. Doster, W.; Cusack, S.; Petry, W. Nature (London) 1989, 337, 754; Phys. Rev. Lett. 1990, 65, 180.
30. Doster, W.; Cusack, S.; Petry, W. Nature (London) 1989, 337, 754; Phys. Rev. Lett. 1990, 65, 180.
31. Young, R. D.; Frauenfelder, H.; Johnson, J. B.; Lamb, D. C.; Nienhaus, G. U.; Phillip, R.; Scholl, R. Chem. Phys. 1991, 158, 315.
32. Ormos, P.; Anasan, A.; Braunstein, D.; Cowen, B. R.; Frauenfelder, H.; Hong, M. K.; Iben, I. E. T.; Sauke, T. B.; Steinbach, P. J.; Young, R. D. Biophys. J. 1990, 57, 191.
33. For a Review, see: McGammon, J. A.; Harvey, S. C. Dynamics of Proteins and Nucleic Acids; Cambridge University Press: Cambridge, 1987.
34. For a Review, see: Gorenstein, D. G. Chem. Rev. 1994, 94, 1315.
35. Ruedisser, S.; Hallbrucker, A.; Mayer, E.; Johari, G. P. J. Phys. Chem. 1997, 101, 266.
36. Ferrari, C.; Johari, G. P. Int. J. Biol. Macromol. In press.
37. Morozov, V. N.; Govorkian, S. G. Bioploymer 1985, 24, 1785.
38. Carerri, G.; Giansanti, A.; Rupley, J. A. Proc. Natl. Acad. Sci. U.S.A. 1986, 83, 6810.
39. Austen, R. H.; Beeson, K. W.; Eisenstein, L.; Frauenfelder, H.; Gunasalus, I. C. Biochemistry 1975, 14, 5355.
40. Noel, T. R.; Parker, R.; Ring, S. G.; Tetham, A. S. Int. J. Biol. Macromol. 1995, 17, 81.
41. Mayer, E. J. Phys. Chem. 1994, 116, 10571.
42. Mayer, E. Biophys. J. 1994, 67, 862.
43. Doster, W.; Kleinert, T.; Post, F., Settles, M. Effect of Solvent on Protein Internal Dynamics: The Kinetics of Ligand Binding to Myoglobin. In Protein Solvent Interactions; Gregory, R. B., Ed.; Marcel-Dekker, Inc: New York, 1994; and references therein.
44. Ben-Naim, A. Solvent Effects on Protein Stability and Protein Association. In Protein Solvent Interactions; Gregory, R. B., Ed.; Marcel-Dekker, Inc: New York, 1994; and references cited therein.
45. Sochava, I. V.; Tseretoli, G. I.; Smirnova, S. I. Biofizika 1991, 36.
46. Douslin, D. R.; Huffman, H. M. J Am. Chem. Soc. 1946, 68, 1704.
47. Adachi, K.; Suga, H.; Seki, S. Bull. Chem. Soc. Jpn. 1971, 44, 78.
48. Angell, C. A. Science 1995, 267, 1924.
49. Frick, B.; Richter, D. Science 1995, 267, 1939.
50. Ediger, M. D.; Angell, C. A.; Nagel, S. R. J. Phys. Chem. 1996, 100, 13200.
51. Johari, G. P. Am. N. Y. Acad. Sci. 1976, 279, 101; Philos. Mag. A 1980, 41, 41.
52. Johari, G. P. Am. N. Y. Acad. Sci. 1976, 279, 101; Philos. Mag. A 1980, 41, 41.
53. Goldstein, M. J. Chem. Phys. 1976, 69, 4767.
54. Gujrati, P. D.; Goldstein, M. J. Chem. Phys. 1980, 84, 859.
55. Cavaille, J.-Y.; Perez, J.; Johari, G. P. Phys. Rev. B 1989, 39, 2411.
56. Johari, G. P.; Perez, J. Mol. Phys. 1994, 83, 235.