Preferences help
enabled [disable] Abstract
Number of results
2002 | 101 | 5 | 647-658
Article title

Small Angle X-Rays Scattering Studies of Biomolecules

Title variants
Languages of publication
The building units of biological systems, the biomolecules, cannot easily be organized or even classified into defined categories. They can be as simple as water or complex as tintin, a muscle protein extremely large with several thousand atoms. To understand their function, one must know their characteristics, where they occur and what they do. One approach to reach such an ambitious task is to determine their structure, as single molecules or assembled into aggregates. Small angle X-ray scattering is the most important method for this purpose. We present studies carried out on several systems, and aiming at different questions about them. We start with lipids, the main components of the cell membranes. These membranes form the cell boundaries, the moiety required for the so-called membrane proteins, but also influence significantly several aspects of biological activity. More complex systems like a muscle fibre is also presented, showing that changes in the structure are related to the movement mechanism. It becomes easy to conclude that knowing the structures and the changes occurring in them is an important way to understand the function of biomolecules and therefore their role in the life cycle.
Physical description
  • MPI for Colloids and Interfaces, c/o HASYLAB, Notkestr. 85, 22603 Hamburg, Germany
  • 1. G. Rapp, Acta Phys. Pol. A, 82, 103, 1992
  • 2. I. Pilz, O. Glatter, O. Kratky, Methods in Enzymology, 61, 148, 1979
  • 3. K. Brandenburg, H. Mayer, M.H.J. Koch, J. Weckesser, E.Th. Rietschel, U. Seydel, Eur. J. Biochem., 218, 555, 1993
  • 4. K. Brandenburg, S.S. Funari, M.H.J. Koch, U. Seydel, J. Struct. Biol., 128, 175, 1999
  • 5. S.S. Funari, B. Nuscher, G. Rapp, K. Beyer, Proc. Natl. Acad. Sci., 98, 8938, 2001
  • 6. D. Otten, L. Lobbecke, K. Beyer, Biophys. J., 68, 584, 1995
  • 7. S.S. Funari, C. di Vita, G. Rapp, Acta Phys. Pol. A, 91, 953, 1997
  • 8. S.S. Funari, Eur. Biophys. J., 27, 590, 1998
  • 9. S.S. Funari, B. Madler, G. Rapp, Eur. Biophys. J., 24, 293, 1996
  • 10. M.A. Bagni, G. Cecchi, P.J. Griffiths, Y. Maeda, G. Rapp, C.C. Ashley, Biophys. J., 67, 1965, 1994
  • 11. V. Lombardi, G. Piazzesi, M.A. Ferenczi, H. Thirlwell, I. Dobbie, M. Irving, Nature, 374, 553, 1995
  • 12. M.A. Bagni, B. Colombini, H. Amenitsch, S. Bernstorff, C.C. Ashley, G. Rapp, P.J. Griffiths, Biophys. J., 80, 2809, 2001
  • 13. G. Piazzesi, V. Lombardi, M.A. Ferenczi, H. Thirlwell, I. Dobbie, M. Irving, Biophys J., 68, Suppl, 92S, 1995
  • 14. L.A. Feigin, D.I. Svergun, Structure Analysis by Small-Angle X-ray and Neutron Scattering, Plenum Press, New York 1987
  • 15. D.I. Svergun, V.V. Volkov, M.B. Kozin, H.B. Stuhrmann, Acta Crystallogr. A, 52, 419, 1996
  • 16. D.I. Svergun, Biophys. J., 76, 2879, 1999
  • 17. S.S. Funari, G. Rapp, M. Perbrandt, K. Dierks, M. Vallazza, C. Betzel, V.A. Erdmann, D.I. Svergun, J. Biol. Chem., 275, 31283, 2000
  • 18. R.K. Hartmann, D.W. Vogel, R.T. Walker, V.A. Erdmann, Nucleic Acids Res., 16, 3511, 1988
  • 19. D.I. Svergun, K.H. Nierhaus, J. Biol. Chem., 275, 14432, 2000
  • 20. E. Westhof, P. Romby, P.J. Romaniuk, J.P. Ebel, C. Ehresmann, B. Ehresmann, J. Mol. Biol., 207, 417, 1989
Document Type
Publication order reference
YADDA identifier
JavaScript is turned off in your web browser. Turn it on to take full advantage of this site, then refresh the page.