| Autor: |
Mentler, Matthias, Weiss, Andreas, Grantner, Klaus, del Pino, Pablo, Deluca, Dominga, Fiori, Stella, Renner, Christian, Meyer Klaucke, Wolfram, Moroder, Luis, Bertsch, Uwe, Kretzschmar, Hans A., Tavan, Paul, Parak, Fritz G. |
| Předmět: |
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| Zdroj: |
European Biophysics Journal; Mar2005, Vol. 34 Issue 2, p97-112, 16p, 1 Black and White Photograph, 1 Diagram, 4 Charts, 6 Graphs |
| Abstrakt: |
Since high-intensity synchrotron radiation is available, “extended X-ray absorption fine structure” spectroscopy (EXAFS) is used for detailed structural analysis of metal ion environments in proteins. However, the information acquired is often insufficient to obtain an unambiguous picture. ENDOR spectroscopy allows the determination of hydrogen positions around a metal ion. However, again the structural information is limited. In the present study, a method is proposed which combines computations with spectroscopic data from EXAFS, EPR, electron nuclear double resonance (ENDOR) and electron spin echo envelope modulation (ESEEM). From EXAFS a first picture of the nearest coordination shell is derived which has to be compatible with EPR data. Computations are used to select sterically possible structures, from which in turn structures with correct H and N positions are selected by ENDOR and ESEEM measurements. Finally, EXAFS spectra are re-calculated and compared with the experimental data. This procedure was successfully applied for structure determination of the Cu2+ complex of the octapeptide repeat of the human prion protein. The structure of this octarepeat complex is rather similar to a pentapeptide complex which was determined by X-ray structure analysis. However, the tryptophan residue has a different orientation: the axial water is on the other side of the Cu. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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