Skip to main content

Advertisement

Journal for Biophysical Chemistry

Biointerphases Cover Image

Collective molecular dynamics in proteins and membranes (Review)

Article metrics

  • 422 Accesses

  • 8 Citations

Abstract

The understanding of dynamics and functioning of biological membranes and, in particular, of membrane embedded proteins is one of the most fundamental problems and challenges in modern biology and biophysics. In particular, the impact of membrane composition and properties and of structure and dynamics of the surrounding hydration water on protein function is an upcoming topic, which can be addressed by modern experimental and computational techniques. Correlated molecular motions might play a crucial role for the understanding of, for instance, transport processes and elastic properties, and might be relevant for protein function. Experimentally that involves determining dispersion relations for the different molecular components, i.e., the length scale dependent excitation frequencies and relaxation rates. Only very few experimental techniques can access dynamical properties in biological materials on the nanometer scale, and resolve dynamics of lipid molecules, hydration water molecules, and proteins and the interaction between them. In this context, inelastic neutron scattering turned out to be a very powerful tool to study dynamics and interactions in biomolecular materials up to relevant nanosecond time scales and down to the nanometer length scale. The author reviews and discusses inelastic neutron scattering experiments to study membrane elasticity and protein-protein interactions of membrane embedded proteins.

References

  1. 1

    M. C. Rheinstädter, T. Seydel, W. Häußler, and T. Salditt, J. Vac. Sci. Technol. A 24, 1191 (2006).

  2. 2

    Structure and Dynamics of Membranes, Handbook of Biological Physics Vol. 1, edited by R. Lipowsky and E. Sackmann (Elsevier, Amsterdam, 1995).

  3. 3

    T. Salditt, Curr. Opin. Colloid Interface Sci. 5, 19 (2000).

  4. 4

    S. Krueger, Curr. Opin. Colloid Interface Sci. 6, 111 (2001).

  5. 5

    T. Salditt, J. Phys.: Condens. Matter 17, R287 (2005).

  6. 6

    H. Frauenfelder, S. Sligar, and P. Wolynes, Science 254, 1598 (1991).

  7. 7

    P. Fenimore, H. Frauenfelder, B. McMahon, and R. Young, Proc. Natl. Acad. Sci. U.S.A. 101, 14408 (2004).

  8. 8

    T. Bayerl, Curr. Opin. Colloid Interface Sci. 5, 232 (2000).

  9. 9

    M. Tarek, D. Tobias, S.-H. Chen, and M. Klein, Phys. Rev. Lett. 87, 238101 (2001).

  10. 10

    J. S. Hub, T. Salditt, M. C. Rheinstädter, and B. L. de Groot, Biophys. J. 93, 3156 (2007).

  11. 11

    {au{gnP.} {pade} {fnGennes}}, {btThe Physics of Liquid Crystals} ({pmClarendon}, {plOxford}, {dy1974}).

  12. 12

    E. Kats, V. Lebedev, and A. Muratov, Phys. Rep. 228, 1 (1993).

  13. 13

    R. Ribotta, D. Salin, and G. Durand, Phys. Rev. Lett. 32, 6 (1974).

  14. 14

    M. C. Rheinstädter, W. Häussler, and T. Salditt, Phys. Rev. Lett. 97, 048103 (2006).

  15. 15

    M. C. Rheinstädter, K. Schmalzl, K. Wood, and D. Strauch, e-print arXiv:0803.0959.

  16. 16

    S. König, W. Pfeiffer, T. Bayerl, D. Richter, and E. Sackmann, J. Chem. Phys. 2, 1589 (1992).

  17. 17

    S. König, E. Sackmann, D. Richter, R. Zorn, C. Carlile, and T. Bayerl, J. Chem. Phys. 100, 3307 (1994).

  18. 18

    S. König, T. Bayerl, G. Coddens, D. Richter, and E. Sackmann, Biophys. J. 68, 1871 (1995).

  19. 19

    W. Pfeiffer, T. Henkel, E. Sackmann, and W. Knorr, Europhys. Lett. 8, 201 (1989).

  20. 20

    W. Pfeiffer, S. König, J. Legrand, T. Bayerl, D. Richter, and E. Sackmann, Europhys. Lett. 23, 457 (1993).

  21. 21

    E. Lindahl and O. Edholm, Biophys. J. 79, 426 (2000).

  22. 22

    A. Nevzorov and M. Brown, J. Chem. Phys. 107, 10288 (1997).

  23. 23

    M. Bloom and T. Bayerl, Can. J. Phys. 73, 687 (1995).

  24. 24

    T. Takeda, Y. Kawabata, H. Seto, S. Komura, S. Gosh, M. Nagao, and D. Okuhara, J. Phys. Chem. Solids 60, 1375 (1999).

  25. 25

    R. Hirn, T. Bayerl, J. Rädler, and E. Sackmann, Faraday Discuss. 111, 17 (1999).

  26. 26

    R. B. Hirn and T. M. Bayerl, Phys. Rev. E 59, 5987 (1999).

  27. 27

    M. F. Hildenbrand and T. M. Bayerl, Biophys. J. 88, 3360 (2005).

  28. 28

    S. Chen, C. Liao, H. Huang, T. Weiss, M. Bellisent-Funel, and F. Sette, Phys. Rev. Lett. 86, 740 (2001).

  29. 29

    M. C. Rheinstädter, C. Ollinger, G. Fragneto, F. Demmel, and T. Salditt, Phys. Rev. Lett. 93, 108107 (2004).

  30. 30

    {btNeutron Spin Echo}, edited by {ei{gnF.} {fnMezei}} ({pmSpringer}, {plBerlin}, {dy1980}).

  31. 31

    A. Caillé, C. R. Seances Acad. Sci., Ser. B 274, 891 (1972).

  32. 32

    N. Lei, C. Safinya, and R. Bruinsma, J. Phys. II 5, 1155 (1995).

  33. 33

    Y. Lyatskaya, Y. Liu, S. Tristram-Nagle, J. Katsaras, and J. F. Nagle, Phys. Rev. E 63, 011907 (2000).

  34. 34

    T. Salditt, M. Vogel, and W. Fenzl, Phys. Rev. Lett. 90, 178101 (2003).

  35. 35

    H. Bary-Soroker and H. Diamant, Europhys. Lett. 73, 871 (2006).

  36. 36

    H. Bary-Soroker and H. Diamant, Phys. Rev. E 76, 042401 (2007).

  37. 37

    C. Ollinger, D. Constantin, J. Seeger, and T. Salditt, Europhys. Lett. 71, 311 (2005).

  38. 38

    H. I. Petrache, N. Gouliaev, S. Tristram-Nagle, R. Zhang, R. M. Suter, and J. F. Nagle, Phys. Rev. E 57, 7014 (1998).

  39. 39

    G. Pabst, J. Katsaras, V. A. Raghunathan, and M. Rappolt, Langmuir 19, 1716 (2003).

  40. 40

    A. Schäfer, T. Salditt, and M. C. Rheinstädter, Phys. Rev. E 77, 021905 (2008).

  41. 41

    F. Chen, W. Hung, and H. Huang, Phys. Rev. Lett. 79, 4026 (1997).

  42. 42

    J. Nagle, H. Petrache, N. Gouliaev, S. Tristram-Nagle, Y. Liu, R. Suter, and K. Gawrisch, Phys. Rev. E 58, 7769 (1998).

  43. 43

    P. Mason, J. Nagle, R. Epand, and J. Katsaras, Phys. Rev. E 63, 030902(R) (2001).

  44. 44

    A. F. Xie, R. Yamada, A. A. Gewirth, and S. Granick, Phys. Rev. Lett. 89, 246103 (2002).

  45. 45

    F. Tokumasu, A. Jin, and A. Dvorak, J. Electron Microsc. 51, 1 (2002).

  46. 46

    G. Pabst, H. Amenitsch, D. Kharakoz, P. Laggner, and M. Rappolt, Phys. Rev. E 70, 021908 (2004).

  47. 47

    V. Kurkal-Siebert, R. Agarwal, and J. C. Smith, Phys. Rev. Lett. 100, 138102 (2008).

  48. 48

    L. Meinhold, J. C. Smith, A. Kitao, and A. H. Zewail, Proc. Natl. Acad. Sci. U.S.A. 104, 17261 (2007).

  49. 49

    U. Haupts, J. Tittor, and D. Oesterhelt, Annu. Rev. Biophys. Biomol. Struct. 28, 367 (1999).

  50. 50

    P. A. Kralchevsky, Adv. Biophys. 34, 25 (1997).

  51. 51

    K. Bohinc, V. Kralj-Iglič, and S. May, J. Chem. Phys. 119, 7435 (2003).

  52. 52

    P. Biscari and F. Bisi, Eur. Phys. J. E 6, 381 (2002)

  53. 53

    P. Lagüe, M. J. Zuckermann, and B. Roux, Biophys. J. 81, 276 (2001).

  54. 54

    N. Dan, P. Pincus, and S. Safran, Langmuir 9, 2768 (1993).

  55. 55

    J. Baudry, E. Tajkhorshid, F. Molnar, J. Phillips, and K. Schulten, J. Phys. Chem. 105, 905 (2001).

  56. 56

    J. F. Hunt, P. D. McCrea, G. Zaccaï, and D. M. Engelman, J. Mol. Biol. 273, 1004 (1997).

  57. 57

    The molecular weight of a BR monomer is 26.9 kDa Ref. 56. Because 1 kg=6.0221×1026 Dalton, the BR trimer thus weighs m tr =1.34 ×10−22 kg.

  58. 58

    http://commons.wikimedia.org/wiki/Image:Cell_membrane_detailed_ diagram.svg

Download references

Author information

Rights and permissions

Reprints and Permissions

About this article