The pressure-temperature phase diagram of hen lysozyme at low pH

Biophysics

Volumn 5, Issue , 2009, Pages 1-9

  Maeno, Akihiro ^a,b   Matsuo, Hiroshi ^a,c   Akasaka, Kazuyuki ^a,b  

^a KINKI UNIVERSITY   (Japan)

^b RIKEN SPring 8 Center ^*  (Japan)

^c Niigata Industrial Creation Organization   (Japan)

Author keywords

Free energy landscape; Hen lysozyme; High pressure fluorescence; High pressure NMR; Thermodynamic stability on pressuretemperature axes

Indexed keywords

EID: 70350065969     PISSN: None     EISSN: 13492942     Source Type: Journal    
DOI: 10.2142/biophysics.5.1     Document Type: Article

References (34)

1. Moriarty, D. F. & Colon, W. Structural intermediates of globular proteins as precursors to amyloid formation. Amyloid Proteins 1 (Jen D. Sipe ed.) vol.1, (Wiley-VCH, 2005).
2. Privolov, P. L. Thermodynamic problems of protein structure. Annu. Rev. Biophys. Chem. vol.18, 47-69 (1989).
3. Privolov, P. L. Cold denaturation of proteins. Crit Rev Biochem Mol Biol. 25, 281-305 (1990).
4. Zipp, A. & Kauzmann, W. Pressure denaturation of metmyoglobin. Biochemistry 12, 4217-4228 (1973).
5. Nash, D. P. & Jonas, J. Structure of pressure-assisted cold denatured lysozyme and comparison with lysozyme folding intermediates. Biochemistry 36, 14375-14383 (1997).
6. Akasaka, K. Probing conformational fluctuation of proteins by pressure perturbation. Chem. Rev. 106, 1814-1835 (2006).
7. Hayashi, R. Trends in high pressure bioscience and biotechnology. Progress in Biotechnology vol.19 (Elsevier, 2002).
8. Matagne, A. & Dobson, C. M. The folding process of hen lysozyme: a perspective from the 'new view'. Cell Mol Life Sci. 54, 363-371 (1998).
9. Radford, S. E., Dobson, C. M. & Evans, P. A. The folding of hen lysozyme involves partially structured intermediates and multiple pathways. Nature 23, 302-307 (1992).
10. Frare, E., Plverino de Laureto, P. Zurdo, J., Dobson, C. M. & Fontana, A. A highly amyloidogenic region of hen lysozyme. J. Mol. Biol. 340, 1153-1165 (2004).
11. Arnaudov, L. N. & Renko de Vries. Thermally induced fibrillar aggregation of hen Egg white lysozyme. Biophys. J. 88, 515-526 (2005).
12. Mishra, R., Sörgjerd, K., Nyström, S., Nordigården, A., Yu, Y. & Hammarström, P. Lysozyme amyloidogenesis is accelerated by specific nicking and fragmentation but decelerated by intact protein binding and conversion. J. Mol. Biol. 366, 1029-1044 (2007).
13. Sasaki, K., Nakatsuka, K., Hayashi, I., Shah, B. R., Morimoto, K. & Akasaka, K. Efficient conversion of intact hen lysozyme into amyloid fibrils by seeding. J. Biol. Macromol. 8, 11-18 (2008).
14. Akasaka, K., Abdul Latif, A., Nakamura, A., Matsuo, K., Tachibana, H. & Gekko, K. Amyloid protofibril is highly voluminous and compressible. Biochemistry 46, 10444-10450 (2007).
15. Abdul Latif, A., Kono, R., Tachibana, H. & Akasaka, K. Kinetic analysis of amyloid protofibril dissociation and volumetric properties of the transition state. Biophys. J. 92, 323-329 (2007).
16. Blake, C. C., Koenig, D. F., Mair, G. A., North, A. C, Phillips, D. C. & Sarma, V. R. Structure of hen egg-white lysozyme. A three-dimensional Fourier synthesis at 2 angstrom resolution. Nature 22, 757-761 (1965).
17. Schwalbe, H., Grimshaw, S. B., Spencer, A., Buck, M., Boyd, J., Dobson, C. M., Redfield, C. & Smith, L. J. A refined solution structure of hen lysozyme determined using residual dipolar coupling data. Protein Sci. 10, 677 (2001).
18. Kitamura, Y. & Itoh, T. Reaction volume of protonic ionization for buffering agents. Prediction of pressure dependence of pH and pOH. Journal of Solution Chemistry 16, 715-726 (1987).
19. Bridgman, P.W. Water in the liquid and five solid forms under pressure. Proc. Am. Acad. Arts Sci. 47, 441-558 (1912).
20. Akasaka, K. & Yamada, H. On-Line cell high pressure nuclear magnetic resonance technique: application to protein studies, in Methods in Enzymology, vol.338: Nuclear Magnetic Resonance of Biological Macromolecules, Part A (James, T. L., et al., eds.), pp. 134-158 (Academic Press, New York, 2001).
21. Yamada, H., Nishikawa, K., Honda, M., Shimura, T., Tabayashi, K. & Akasaka, K. Pressure-resisting cell for highpressure, high-resolution nuclear magnetic resonance measurements at very high magnetic fields. Rev. Sci. Instrum. 72, 1463-1471 (2001). (Pubitemid 33605561)
22. Royer, C. A. Probing protein folding and conformational transitions with fluorescence. Chem. Rev. 106, 1769-1784 (2006).
23. Kamatari, Y. O., Yamada, H., Akasaka, K., Jones, J. A., Dobson, C. M & Smith, L. J. Response of native and denatured henlysozyme to high pressure studied by 15N/1H NMR spectroscopy. Eur. J. Biochem. 268, 1782-1793 (2001).
24. Refaee, M., Tezuka, T., Akasaka, K. & Williamson, M. P. Pressure-dependent changes in the solution structure of hen egg-white lysozyme. J. Mol. Biol. 327, 857-865 (2003).
25. Wishart, D. S., Bigam, C. G., Holm, A., Hodges, R. S. & Sykes, B. D. 1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearestneighbor effects. J. Biomol. NMR 5, 67-81 (1995).
26. Redfield, C. & Dobson, C. M. Sequential 1H NMR assignments and secondary structure of hen egg white lysozyme in solution. Biochemistry 27, 122-136 (1988).
27. Lakowicz, J. R. Principles of Fluorescence Spectroscopy (Third Edition) (Springer, 2006).
28. Lassalle, M.W., Yamada, H. & Akasaka, K. The pressuretemperature free energy-landscape of Staphylococcal nuclease monitored by 1H NMR. J. Mol. Biol. 298, 293-302 (2000).
29. Brandts, J. F. Olivera, R. J. & Westort, C. Thermodynamics of protein denaturation. Effect of pressure on the denaturation of ribonuclease A. Biochemistry 9, 1038-1047 (1970).
30. Hawley, S. A. Reversible pressure-temperature denaturation of chymotrypsinogen. Biochemistry 10, 2436-2442 (1971).
31. Panick, G., Malessa, R., Winter, R., Rapp, G., Frye, K. J. & Royer, C. A. Structural characterization of the pressuredenatured state and unfolding/refolding kinetics of staphylococcal nuclease by synchrotron small-angle X-ray scattering and Fourier-transform infrared spectroscopy. J. Mol. Biol. 16, 389-402 (1998).
32. Panick, G., Vidugiris, G. J. A., Malessa, R., Rapp, G., Winter, R. & Royer, C. A. Exploring the temperature-pressure phase diagram of Staphylococcal Nuclease. Biochemistry 38, 4157-4164 (1999).
33. Ravindra, R. & Winter, R. On the temperature-pressure freeenergy landscape of protein. Chem. Phys. Chem. 4, 359-365 (2003).
34. Sasahara, K., Sakurai, M. & Nitta, K. Pressure effect on denaturant-induced unfolding of hen egg white lysozyme. Proteins 15, 180-187 (2001).