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Volume 18 (2004), Issue 2, Pages 323-330

Vibrational spectroscopy and computer modeling of proteins: solving structure of α1-acid glycoprotein

Vladimír Kopecký,1,2 Rüdiger Ettrich,3 Kateřina Hofbauerová,2 and Vladimír Baumruk1

1Institute of Physics, Charles University, Ke Karlovu 5, CZ-12116 Prague 2, Czech Republic
2Department of Biochemistry, Faculty of Science, Charles University, Albertov 2030, CZ-12840 Prague 2, Czech Republic
3Laboratory of High Performance Computing, Institute of Physical Biology USB and Institute of Landscape Ecology AS CR, Zámek 136, CZ-37333 Nové Hrady, Czech Republic

Copyright © 2004 Hindawi Publishing Corporation. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


This work introduces a new approach connecting vibrational spectroscopy with homology and energetic molecular modeling of proteins. Combination of both methods can compensate their disadvantages and result in realistic three-dimensional protein models. The approach is most powerful for membrane proteins or glycoproteins with high carbohydrate content where X-ray or NMR analysis is not always successful. Nevertheless, it can also serve as a tool of preliminary analysis of any protein with unknown structure. Power of the approach is demonstrated on human α1-acid glycoprotein. Its predicted structure published in [V. Kopecký Jr. et al., Biochem. Biophys. Res. Commun. 300 (2003), 41–46] is discussed in detail with respect to the approach and its general employment.