
Proceedings Paper
Functional dynamics of hydrolytic enzymesFormat | Member Price | Non-Member Price |
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Paper Abstract
One of important stages of the substrate bond breaking in the active site (AS) of α-chymotrypsin (ACT) is considered. Three tasks are solved by methods of quantum mechanics and stochastic molecular dynamics: the loosening of peptide bond of a substrate attacked by O- ion of Ser195 of catalytic group; the opportunity of increase of a peptide bond (PB) breaking probability; the increase of this probability related to nonlinear interacting modes (or Fermi resonance (FR)) of oscillations of group N-H in PB. It is shown also that the splitting of vibrational levels Amide A and Amide B in a spectrum of an amide group pays off due to FR.
Paper Details
Date Published: 13 October 2003
PDF: 11 pages
Proc. SPIE 5068, Saratov Fall Meeting 2002: Optical Technologies in Biophysics and Medicine IV, (13 October 2003); doi: 10.1117/12.518626
Published in SPIE Proceedings Vol. 5068:
Saratov Fall Meeting 2002: Optical Technologies in Biophysics and Medicine IV
Valery V. Tuchin, Editor(s)
PDF: 11 pages
Proc. SPIE 5068, Saratov Fall Meeting 2002: Optical Technologies in Biophysics and Medicine IV, (13 October 2003); doi: 10.1117/12.518626
Show Author Affiliations
Alexey V. Kargovsky, M.V. Lomonosov Moscow State Univ. (Russia)
Olga P. Khodjer, M.V. Lomonosov Moscow State Univ. (Russia)
Olga P. Khodjer, M.V. Lomonosov Moscow State Univ. (Russia)
Yury M. Romanovsky, M.V. Lomonosov Moscow State Univ. (Russia)
Published in SPIE Proceedings Vol. 5068:
Saratov Fall Meeting 2002: Optical Technologies in Biophysics and Medicine IV
Valery V. Tuchin, Editor(s)
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