13 October 2003 Functional dynamics of hydrolytic enzymes
Author Affiliations +
Proceedings Volume 5068, Saratov Fall Meeting 2002: Optical Technologies in Biophysics and Medicine IV; (2003) https://doi.org/10.1117/12.518626
Event: Saratov Fall Meeting 2002 Laser Physics and Photonics, Spectroscopy, and Molecular Modeling III; Coherent Optics of Ordered and Random Media III, 2002, Saratov, Russian Federation
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.
© (2003) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
Alexey V. Kargovsky, Alexey V. Kargovsky, Olga P. Khodjer, Olga P. Khodjer, Yury M. Romanovsky, Yury M. Romanovsky, } "Functional dynamics of hydrolytic enzymes", Proc. SPIE 5068, Saratov Fall Meeting 2002: Optical Technologies in Biophysics and Medicine IV, (13 October 2003); doi: 10.1117/12.518626; https://doi.org/10.1117/12.518626
PROCEEDINGS
11 PAGES


SHARE
Back to Top