Nonlinear Model of the Specificity of DNA-Protein Interactions and Its Stability
Autor: | R Khairani, Donny Dwiputra, Wahyu Hidayat, Freddy P. Zen |
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Rok vydání: | 2016 |
Předmět: |
chemistry.chemical_classification
Quantitative Biology::Biomolecules History Base pair Hydrogen bond Peptide Quantitative Biology::Genomics 01 natural sciences 010305 fluids & plasmas Computer Science Applications Education Quantitative Biology::Subcellular Processes chemistry.chemical_compound symbols.namesake chemistry Computational chemistry Chemical physics Nonlinear model 0103 physical sciences symbols Binding site 010306 general physics Hamiltonian (quantum mechanics) DNA Morse potential |
Zdroj: | Journal of Physics: Conference Series. 739:012030 |
ISSN: | 1742-6596 1742-6588 |
DOI: | 10.1088/1742-6596/739/1/012030 |
Popis: | Specific DNA-protein interactions are fundamental processes of living cells. We propose a new model of DNA-protein interactions to explain the site specificity of the interactions. The hydrogen bonds between DNA base pairs and between DNA-protein peptide groups play a significant role in determination of the specific binding site. We adopt the Morse potential with coupling terms to construct the Hamiltonian of coupled oscillators representing the hydrogen bonds in which the depth of the potentials vary in the DNA chain. In this paper we investigate the stability of the model to determine the conditions satisfying the biological circumstances of the DNA-protein interactions. |
Databáze: | OpenAIRE |
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