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Energy transfer along α‐helical proteins
Author(s) -
Palma Rocio
Publication year - 1992
Publication title -
international journal of quantum chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.484
H-Index - 105
eISSN - 1097-461X
pISSN - 0020-7608
DOI - 10.1002/qua.560440716
Subject(s) - excited state , chemistry , hamiltonian (control theory) , molecule , exciton , vibrational energy , potential energy , molecular physics , atomic physics , chemical physics , physics , quantum mechanics , mathematical optimization , mathematics , organic chemistry
The aim of this paper was to establish a distribution function for the number of vibrational excitons in a given state N ( r , k ) for describing the energy‐transfer process along α‐helical proteins under normal physiological conditions. In the background lies Davydov's model, where the most important role is placed by the amide‐I bond (CO). In this protein, the peptide group molecules are localized along three chains, which are relatively tightly linked by hydrogen bonds. Their vibrations are weakly connected with other normal vibrations. The Hamiltonian of such a chain is expressed in terms of the second quantization in the approximation when only one molecule is excited by the energy of hydrolysis of ATP and transfers its energy to the neighboring molecules. The further development of the model is made using Boltzman's equation in the stationary case at high temperatures T /ω ≫ 1. We determined the temperature dependence of the energy flux. The best result was that the process of energy transfer is determined, principally, by the vibrational exciton–phonon interaction. © 1992 John Wiley & Sons, Inc.