Picosecond Internal Dynamics of Lysozyme As Affected by Thermal Unfolding in Nonaqueous Environment

Biophysical Journal

Volumn 86, Issue 1 I, 2004, Pages 480-487

  De Francesco, A ^a   Marconi, M ^a   Cinelli, S ^a   Onori, G ^a   Paciaroni, Alessandro ^a  

^a UNIVERSITY OF PERUGIA   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

GLYCEROL; LYSOZYME; POLYPEPTIDE; PROTEIN;

AQUEOUS SOLUTION; ARTICLE; DENATURATION; ELASTICITY; ENZYME STRUCTURE; FUNCTIONAL ASSESSMENT; HYDRODYNAMICS; LOW TEMPERATURE PROCEDURES; MELTING POINT; MOLECULAR DYNAMICS; MOTION; NEUTRON SCATTERING; NONHUMAN; PROTEIN FOLDING; SOLVATION; SPECTROSCOPY; TEMPERATURE MEASUREMENT; THERMAL ANALYSIS; TIME; VIBRATION;

GOES;

EID: 0346688701     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(04)74126-0     Document Type: Article

References (49)

1. Andreani, C., A. Filabozzi, F. Menzinger, A. Desideri, A. Deriu, and D. Di Cola. 1995. Dynamics of hydrogen atoms in superoxide dismutase by quasielastic neutron scattering. Biophys. J. 68:2519-2523.
2. Bée, M. 1988. Quasielastic Neutron Scattering. Adam Hilger, Bristol, UK and Philadelphia, PA.
3. Bell, L. N., M. J. Hageman, and L. M. Muraoka. 1995. Thermally induced denaturation of lyophilized bovine somatotropin and lysozyme as impacted by moisture and excipients. J. Pharmacol. Sci. 84:707-712.
4. Burova, T. V., N. V. Grinberg, V. Y. Grinberg, R. V. Rariy, and A. M. Klibanov. 2000. Calorimetric evidence for a native-like conformation of hen egg-white lysozyme dissolved in glycerol. Biochim. Biophys. Acta. 1478:309-317.
5. Caliskan, G., A. Kisliuk, A. M. Tsai, C. L. Soles, and A. P. Sokolov. 2003. Protein dynamics in viscous solvents. J. Chem. Phys. 118:4230-4236.
6. Cordone, L., M. Ferrand, E. Vitrano, and G. Zaccai. 1999. Harmonic behaviour of trehalose-coated carbon-monoxy-myoglobin at high temperature. Biophys. J. 76:1043-1047.
7. Cusack, S. 1989. Low frequency dynamics of proteins: comparison of inelastic neutron scattering results with theory. Chem. Scr. 29A:103-107.
8. Cusack, S., and W. Doster. 1990. Temperature dependence of the low frequency dynamics of myoglobin. Biophys. J. 58:243-251.
9. Diehl, M., W. Doster, W. Petry, and H. Shober. 1997. Water-coupled low frequency modes of myoglobin and lysozyme observed by inelastic neutron scattering. Biophys. J. 73:2726-2732.
10. Doster, W., S. Cusack, and W. Petry. 1989. Dynamical transition of myoglobin revealed by inelastic neutron scattering. Nature. 337:754-756.
11. Doster. W., S. Cusack, and W. Petry. 1990. Dynamics instability of liquid like motions in a globular protein observed by inelastic neutron scattering. Phys. Rev. Lett. 65:1080-1083.
12. Drago, G. A., and T. D. Gibson. 2001. Enzyme stability and stabilisation: applications and case studies. In Engineering and Manufacturing for Biotechnology. M. Hofman and P. Thonart, editors. Kluwer Academic Publishers, Dordrecht, Holland. 361-376.
13. Elliot, S. R. 1992. A unified model for the low-energy vibrational behaviour of amourphous solids. Eurphys. Lett. 19:201-206.
14. Ferrand. M., A. Dianoux, and W. Petry. 1993. Thermal motion and function of bacteriorodhopsin. Proc. Natl. Acad. Sci. USA. 90:9668-9672.
15. Fitter, J. 2003. A measure of conformational entropy change during thermal protein unfolding using neutron spectroscopy. Biophys. J. 84:3924-3930.
16. Fitter, J. 1999. The temperature dependence of internal molecular motions in hydrated and dry α-amylase: the role of hydration water in the dynamical transition of proteins. Biophys. J. 76:1034-1042.
17. Fitter, J., R. Herrmann, N. A. Dencher, A. Blume, and T. Hauss. 2001. Activity and stability of a thermostable α-amilase compared to its mesophilic homologue: mechanism of thermal adaptation. Biochemistry. 40:10723-10731.
18. Fitter, J., R. E. Lechner, and N. A. Dencher. 1997. Picosecond molecular motions in bacteriorhodopsin from neutron scattering. Biophys. J. 73:2126-2137.
19. Fitter, J., R. E. Lechner, G. Buldt, and N. A. Dencher. 1996. Internal molecular motions of bacteriorhodopsin: hydration-induced flexibility studied by quasielastic inchoerent neutron scattering using oriented purple membranes. Proc. Natl. Acad. Sci. USA. 93:7600-7605.
20. Frauenfelder, H., and B. McMahon. 1998. Dynamics and function of proteins: the search for general concepts. Proc. Natl. Acad. Sci. USA. 9995:4795-4797.
21. Frauenfelder, H., S. G. Sligar, and P. G. Wolynes. 1991. The energy landscapes and motions of proteins. Science. 254:1598-1603.
22. Frick, B., and D. Richter. 1995. The microscopic basis of the glass transition in polymers from neutron scattering studies. Science. 267:1939-1945.
23. Fujita, Y., and Y. Noda. 1978. Effect of hydration on the thermal denaturation of lysozyme as measured by differential scanning calorimetry. Bull. Chem. Soc. Jpn. 51:1567-1568.
24. Göetze, W. 1991. Liquids, Freezing and the Glass Transition. North Holland, Amsterdam. The Netherlands.
25. Gottfried, D. S., E. S. Peterson, A. G. Sheikh, J. Wang, and J. M. Friedman. 1996. Evidence for damped hemoglobin dynamics in a room temperature trehalose glass. J. Phys. Chem. 100:12034-12042.
26. Gregory, R. B. 1995. Protein-Solvent Interactions. Marcel Dekker, New York.
27. Gregory. R. B., and R. Lumry. 1985. Hydrogen-exchange evidence for distinct structural classes in globular proteins. Biopolymers. 24:301-326.
28. Grigera, T. S., V. Martin-Major, G. Parisi, and P. Verrocchio. 2003. Phonon interpretation of the boson peak in supercooled liquids. Lett. to Nature. 422:289-292.
29. Lichtenegger, H., W. Doster, T. Kleinert, A. Birk, F. Parak, B. Sepiol, and G. Vogl. 1999. Heme-solvent coupling, a Mössbauer study of myoglobin in sucrose. Biophys. J. 76:414-422.
30. Lovesey, S. 1988. Theory of Neutron Scattering from Condensed Matter. Oxford University Press, Oxford, UK.
31. Marques, O., and Y. H. Sanjouand. 1995. Hinge-bending motion in citrate synthase arising from normal modes calculations. Proteins. 23:557-560.
32. Orecchini, A., A. Paciaroni, A. R. Bizzarri, and S. Cannistraro. 2002. Dynamics of different hydrogen classes in β-lactoglobulin: a quasielastic neutron scattering investigation. J. Phys. Chem. B. 106:7348-7354.
33. Paciaroni, A., S. Cinelli, and G. Onori. 2002. Effect of the environment on the protein dynamical transition: a neutron scattering study. Biophys. J. 83:1157-1164.
34. Paciaroni, A., A. Orecchini, S. Cinelli, G. Onori, R. E. Lechner, and J. Pieper. 2003. Proteins dynamics on the picoseconds timescale as affected by the environment: a quasielastic neutron scattering study. Chem. Phys. 292:397-404.
35. Paciaroni, A., M. E. Stroppolo, C. Arcangeli, A. R. Bizzarri, A. Desideri, and S. Cannistraro. 1999. Incoherent neutron scattering of copper azurin: a comparison with molecular dynamics simulation results. Eur. Biophys J. 28:447-456.
36. Rader, A. J., B. M. Hespenheide, L. A. Kuhn, and M. F. Thorpe. 2002. Protein unfolding: rigidity lost. Proc. Natl. Acad. Sci. USA. 99:3540-3545.
37. Receveur, V., P. Calmettes, J. C. Smith, M. Desmadril, G. Coddens, and D. Durand. 1997. Picosecond dynamical changes on denaturation of yeast phosphoglycerate kinase revealed by quasielastic neutron scattering. Proteins. 28:380-387.
38. Russo, D., J. Péz, J. M. Zanotti, M. Desmadril, and D. Durand. 2002. Dynamic transition associated with the thermal dentauration of small beta protein. Biophys. J. 83:2792-2800.
39. Seno, Y., and N. Go. 1990. Deoxymyoglobin studied by the conformational normal mode analysis. 2. The conformational change upon oxygenation. J. Mol. Biol. 216:111-126.
40. Shamblin, S., X. Tang, L. Chang, B. Hancock, and M. Pikal. 1999. Characterization of the time scale of molecular motion in pharmaceutically important glasses. J. Phys. Chem. B. 103:4113-4121.
41. Tang, K. E. S., and K. Dill. 1998. Native protein fluctuations: the conformational-motion temperature and the inverse correlation of protein flexibility with protein stability. J. Biomol. Struct. Dyn. 16:397-411.
42. Tehei, M., D. Madern, C. Pfister, and G. Zaccai. 2001. Fast dynamics of halophilicmalate dehydrogenase and BSA as measured by neutron scattering under various solvent conditions influencing protein stability. Proc. Natl. Acd. Sci. USA. 98:14356-14361.
43. Tsai, A. M., D. A. Neumann, and L. N. Bell. 2000. Molecular dynamics of solid-state lysoyme as affected by glycerol and water: a neutron scattering study. Biophys. J. 79:2728-2732.
44. Tsai, A. M., T. J. Udovic, and D. A. Neumann. 2001. The inverse relationship between protein dynamics and thermal stability. Biophys. J. 81:2339-2343.
45. Vitkup, D., D. Ringe, G. A. Petsko, and M. Karplus. 2000. Solvent mobility and the protein "glass" transition. Nat. Struct. Biol. 7:34-38.
46. Volino, F., and A. J. Dianoux. 1980. Neutron incoherent scattering law for diffusion in a potential of spherical symmetry: general formalism and application to diffusion inside a sphere. Mol. Phys. 41:271-279.
47. Walser, R., and W. F. van Gunsteren. 2001. Viscosity dependence of protein dynamics. Proteins. 42:414-421.
48. Williams, G., and D. C. Watts. 1970. Non-symmetrical dielectric relaxation behaviour arising from simple empirical decay function. Trans. Faraday Soc. 66:80-83.
49. Zaks, A., and A. M. Klibanov. 1984. Enzymatic catalysis in organic media at 100°C. Science. 224:1249-1251.