The temperature dependence of internal molecular motions in hydrated and dry α-amylase: The role of hydration water in the dynamical transition of proteins

Biophysical Journal

Volumn 76, Issue 2, 1999, Pages 1034-1042

  Fitter, J ^a,b  

^a FORSCHUNGSZENTRUM JÜLICH   (Germany)

^b DARMSTADT UNIVERSITY OF TECHNOLOGY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLASE; RHODOPSIN;

ARTICLE; ENERGY TRANSFER; HYDRATION; MOLECULAR DYNAMICS; NEUTRON SCATTERING; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN LIPID INTERACTION; PROTEIN STRUCTURE; SPECTROMETER; STOCHASTIC MODEL; TEMPERATURE DEPENDENCE;

EID: 0033064923     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)77268-1     Document Type: Article

References (53)

1. Ansari, A., C. M. Jones, E. R. Henry, J. Hofrichter, and W. A. Eaton. 1995. The role of solvent viscosity in the dynamics of protein conformational changes. Science. 256:1796-1798.
2. Bartunik, H. D., P. Jolles, J. Berthou, and A. J. Dianoux. 1982. Intramolecular Low-frequency vibrations in lysozyme by neutron time-of-flight spectroscopy. Biopolymers. 21:43-50.
3. Bee, M. 1988. Quasi-Elasic Neutron Scattering. Adam and Hilger, Philadelphia.
4. Bellissent-Funel, M.-C., J. Teixeira, S. H. Chen, B. Dorner, H. D. Middendorf, and H. L. Crespi. 1989. Low-frequency collective modes in dry and hydrated proteins. Biophys. J. 56:713-716.
5. Benigno, A. J., E. Ahmed, and M. Berg. 1996. The influence of solvent dynamics on the lifetime of solute-solvent hydrogen bonds. J. Chem. Phys. 104:7382-7394.
6. Bizzarri, A. R., C. X. Wang, W. Z. Chen, and S. Cannistraro. 1995. Hydrogen bond analysis by MD simulation of copper plastocyanin at different hydration levels. Chem. Phys. 201:463-472.
7. Brooks, C. L., and M. Karplus. 1989. Solvent effects on protein motion and protein effects on solvent motion. J. Mol. Biol. 208:159-181.
8. Cordone, L., P. Galajda, E. Vitrano, A. Gassmann, A. Ostermann, and F. Parak. 1998. A reduction of protein specific motions in co-ligated myoglobin embedded in a trealose glass. Eur. Biophys. J. 27:173-176.
9. Crowe, L. M., D. S. Reid, and J. H. Crowe. 1996. Is trehalose special for preversing dry biomaterials? Biophys. J. 71:2087-2093.
10. Cusack, S., and W. Doster. 1990. Temperature dependence of the low frequency dyanamics of myoglobin. Biophys. J. 58:243-251.
11. Daniels, B. V., B. P. Schoenborn, and Z. R. Korszun. 1996. Myoglobin solvent structure at different temperatures. Basic Life Sci. 64:325-331.
12. Demel, F., W. Doster, W. Petry, and A. Schulte. 1997. Vibrational frequency shifts as a probe of hydrogen bonds: thermal expansion and glass transition of myoglobin in mixed solvents. Eur. Biophys. J. 26:327-335.
13. Diehl, M., W. Doster, W. Petry, and H. Schober. 1997. Water-coupled low-frequency modes of myoglobin and lysozyme observed by inelastic neutron scattering. Biophys. J. 73:2726-2732.
14. Di Pace, A., A. Cupane, M. Leone, E. Vitrano, and L. Cordone. 1992. Protein dynamics. Biophys. J. 63:475-484.
15. Doster, W., A. Bachleitner, R. Dunau, M. Hiebl, and E. Lüscher. 1986. Thermal prperties of water in myoglobin crystals and solutions at subzero temperatures. Biophys. J. 50:213-219.
16. Doster, W., S. Cusack, and W. Petry. 1989. Dynamical transition of myoglobin revealed by inelastic neutron scattering. Nature. 337: 754-756.
17. Ferrand, M., A. J. Dianoux, W. Petry, and G. Zaccai. 1993. Thermal motions of bacteriorhodopsin in purple membranes. Proc. Natl. Acad. Sci. USA. 90:9668-9672.
18. Finney, J. L., B. J. Gellatly, I. C. Golton, and J. Goodfellow. 1980. Solvent effects and polar interactions in the structural stability and dynamics of globular proteins. Biophys. J. 32:17-30.
19. Finney, J. L., and P. L. Poole. 1984. Protein hydration and enzyme activity: the role of hydration-induced conformation and dynamic changes in the activity of lysozyme. Comments Mol. Cell. Biophys. 2:129-151
20. Fitter J., S. A. W. Verclas, R. E. Lechner, and N. A. Dencher. 1998a. Function and picosecond dynamics of bacteriorhodopsin in purple membrane at different lipidation and hydration. FEBS Lett. 433:321-325.
21. Fitter, J., O. P. Ernst, T. Hauss, R. E. Lechner, K. P. Hofmann, and N. A. Dencher. 1998b. Molecular motions and hydration of purple membranes and disk membranes studied by neutron scattering. Eur. Biophys. J. 27:638-645.
22. Fitter, J., R. E. Lechner, G. Büldt, and N. A. Dencher. 1996. Temperature dependence of molecular motions in the membrane protein bacteriorhodopsin from QINS. Physica B. 226:61-65.
23. Fitter, J., R. E. Lechner, and N. A. Dencher. 1997. Picosecond molecular motions in bacteriorhodopsin from neutron scattering. Biophys. J. 73: 2126-2137.
24. Frauenfelder, H., G. A. Petsko, and D. Tsernoglou. 1979. Temperature-dependent x-ray diffraction as a probe of protein structural dynamics. Nature. 280:558-563.
25. Go, N., T. Noguti, and T. Nishikawa. 1983. Dynamics of a small globular protein in terms of low-frequency vibrational modes. Proc. Natl. Acad. Sci. USA. 80:3696-3700.
26. Green, J. L., J. Fan, and C. A. Angell. 1994. The protein-glass analogy: some insights from homopeptide comparison. J. Phys. Chem. 98: 13780-13790.
27. Hagen, S. J., J. Hofrichter, and W. A. Eaton. 1995. Protein reaction kinetics in a room-temperature glass. Science. 269:959-962.
28. Hofer, K., A. Hallbrucker, E. Mayer, and G. P. Johari. 1989. Vitrified aqueous solutions. 3. Plasticization of water's H-bond network and glass transition temperatures minimum. J. Chem. Phys. 93:4674-4677.
29. Iben, I. E. T., D. Braunstein, W. Doster, H. Frauenfelder, M. K. Hong, J. B. Johnson, S. Luck, P. Ormos, A. Schulte, P. J. Steinbach, A. H. Xie, and R. D. Young. 1989. Glassy behavior of a protein. Phys. Rev. Lett. 62:1916-1919.
30. Kuntz, I. D., and W. Kauzmann. 1974. Hydration of proteins and polypeptides. Adv. Protein Chem. 28:239-345.
31. Lechner, R. E. 1994. Structural aspects of diffusive motions in some complex systems. In Quasielastic Neutron Scattering: Future Prospects on High-Resolution Inelastic Neutron Scattering. J. Colmenero, A. Alegria, and F. J. Bermejo, editors. World Scientific, Singapore. 62-91.
32. 2. Solid State Ionics. 46:25-32.
33. Lechner, R. E., J. Fitter, N. A. Dencher, and T. Hauss. 1998. Dehydration of biological membranes by cooling: an investigation on the purple membrane. J. Mol. Biol. 277:593-603.
34. Martel, P., P. Calmettes, and B. Hennion. 1991. Vibrational modes of hemoglobin in red blood cells. Biophys. J. 59:363-374.
35. Miyazaki, Y., T. Matsuo, and H. Suga. 1993. Glass transition of myoglobin crystal. Chem. Phys. Lett. 213:303-308.
36. Nocek, J. M., E. D. A. Stemp, M. G. Finnegan, T. I. Koshy, M. K. Johnson, E. Margoliash, A. G. Mauk, M. Smith, and B. M. Hoffman. 1991. Low-temperature, cooperative conformational transition within [Zn-cytochrome c peroxidase, cytochrome c] complexes: variation with cytochrome. J. Am. Chem. Soc. 113:6822-6831.
37. Norin, M., F. Haeffner, K. Hult, and O. Edholm. 1994. Molecular dynamics simulation of an enzyme surrounded by vacuum, water, or a hydrophobic solvent. Biophys. J. 67:548-559.
38. Painter, P. C., L. E. Mosher, and C. Rhoads. 1982. Low frequency modes in the Raman spectra of proteins. Biopolymers. 21:1469-1472.
39. Parak, F. 1986. Correlation of protein dynamics with water mobility: Mössbauer spectroscopy and microwave absorption methods. Methods Enzymol. 127:196-206.
40. Parak, F., and H. Frauenfelder. 1993. Protein dynamics. Physica A. 201: 332-345.
41. Parak, F., and E. W. Knapp. 1982. A consistent picture of protein dynamics. Proc. Natl. Acad. Sci. USA. 81:7088-7092.
42. Rasmussen, B. F., A. M. Stock, D. Ringe, and G. A. Petsko. 1992 Crystalline ribonuclease A loses function below the dynamical transition at 220 K. Nature. 357:423-424.
43. Rupley, J. A., and G. Careri. 1991. Protein hydration and function. Adv. Protein Chem. 41:37-172.
44. Shah, N. K., and R. D. Ludescher. 1993. Influence of hydration on the internal dynamics of hen egg white lysozyme in the dry state. Photochem. Photobiol. 58:169-174.
45. Smith, J. C. 1991. Protein dynamics: comparison of simulations with inelastic neutron scattering experiments. Q. Rev. Biophys. 24:227-291.
46. Sochava, I. V. 1997. Heat capacity and thermodynamic characteristics of denaturation and glass transition of hydrated and anhydrous proteins. Biophys. Chem. 69:31-41.
47. Sokolov, A. P. 1997. The glass transition: new ideas in an age-old field. Endeavour. 21:109-113.
48. Sokolov, A. P., J. Hurst, and D. Quitmann. 1995. Dynamics of supercooled water: mode-coupling theory approach. Phys. Rev. B. 51:12865-12868.
49. Steinbach, J. P., and B. R. Brooks. 1994. Protein simulation below the glass-transition temperature. Dependence on cooling protocol. Chem. Phys. Lett. 226:447-452.
50. Steinbach, J. P., and B. R. Brooks. 1996. Hydrated myoglobin's anharmonic fluctuations are not primarily due to dihedral transitions. Proc. Natl. Acad. Sci. USA. 93:55-59.
51. Steinbach, J. P., R. J. Loncharich, and B. R. Brooks. 1991. The effects of environment and hydration on protein dyanmics: a simulation study of myoglobin. Chem. Phys. 158:383-394.
52. Steiner, Th., W. Saenger, and R. E. Lechner. 1991. Dynamics of orientationally disordered hydrogen bonds in a molecular cage. Mol. Phys. 72:1211-1232.
53. Wilden, U., and H. Kühn. 1982. Light-dependent phosphorylation of rhodopsin: number of phosphorylation sites. Biochemistry. 21: 3014-3022.