Preferences help
enabled [disable] Abstract
Number of results
2010 | 117 | 5 | 756-759
Article title

Quantum Foundations of Resonant Recognition Model

Title variants
Languages of publication
Biomolecular recognition is an open scientific problem, which has been investigated in many theoretical and experimental aspects. In that sense, there are encouraging results within Resonant Recognition Model (RRM), based on the finding that there is a significant correlation between spectra of the numerical presentation of amino acids in the primary structure of proteins and their biological activity. It has been found through an extensive research that proteins with the same biological function have a common frequency in their numerical spectra. This frequency was found then to be a characteristic feature for protein biological function or interaction The RRM model proposes that the selectivity of protein interactions is based on resonant energy transfer between interacting biomolecules and that this energy, electromagnetic in its nature, is in the frequency range of 10^{13} to 10^{15} Hz, which incorporates infra-red (IR), visible and a small portion of the ultra-violet (UV) radiation. In this paper, the quantum mechanical basis of the RRM model will be investigated using the solution in the simplified framework of Hückel-like theory of molecular orbits.
Physical description
  • 1. I. Cosic, The Resonant Recognition Model of Macromolecular Bioactivity, Birkhauser, Berlin 1997
  • 2. E. Pirogova, I. Cosic, in: Proc. Biomed. Engin., ACTA Press 2004, p. 417
  • 3. I. Cosic, E. Pirogova, V. Vojisavljević, Q. Fang, Proc. Biomed. Engin., ACTA Press 2007, p. 555
  • 4. D. Raković, M. Dugić, M. Plavšić, Mater. Sci. Forum 494, 513 (2005)
  • 5. I. Cosic, IEEE Trans. Biomed. Engin. 41, 1101 (1994)
  • 6. E. Pirogova, G.P. Simon, I. Cosic, IEEE Trans. NanoBiosci. 2, 63 (2003)
  • 7. E. Pirogova, I. Cosic, Molec. Simulat., 28, 845 (2002)
  • 8. V. Vojisavljevic, E. Pirogova, I. Cosic, Int. J. Rad. Biol. 83, 221 (2007)
  • 9. Q. Fang, I. Cosic, APESM 21, 179 (1998)
  • 10. E. Pirogova, M. Akay, I. Cosic, Proc. IEEE EMBS 21, 1215 (1999)
  • 11. I. Cosic, A.E. Drummond, J.R. Underwood, M.T.W. Hearn, Molec. Cell. Biochem. 130, 1 (1994)
  • 12. V. Krsmanovic, J.M. Biquard, M. Sikorska-Walker, I. Cosic, C. Desgranges, M.A. Trabaud, J.F. Whitfield, J.P. Durkin, A. Achour, M.T. Hearn, J. Peptide Res. 52, 410 (1998)
  • 13. B. Krsmanović, I. Cosić, J.M. Biquard, M.T.W. Hearn, Artifical peptides and induced antibodies, Patent Appl. PCT/FR 93/00171
  • 14. W. Kutzelnigg, J. Comput. Chem. 28, 25 (2006)
  • 15. J.P. Lowe, K. Peterson, Quantum Chemistry, Elsevier, Amsterdam 2005
  • 16. L.A. Gribov, From Theory of Spectra Towards Theory of Chemical Transformations, URSS, Moscow 2001
  • 17. V.I. Baranov, L.A. Gribov, Zh. Prikl. Spektr. 71, 421 (2004)
  • 18. V.I. Baranov, F.A. Savin, L.A. Gribov, J. Appl. Spectr. 71, 320 (2004)
  • 19. K. Pribram, Brain and Perception: Holonomy and Structure in Figural Processing, Eds. Lawrence Erlbaum, Hillsdale, New York 1991; K. Pribram in: Languages of the Brain Brandon House, New York 1971
  • 20. D. Raković, M. Dugić, M. Plavšić, G. Keković, I. Cosic, D. Davidović, Mater. Sci. Forum 518, 485 (2006)
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.