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Biomedical subjects

J Ladik

Publications and source records attributed to J Ladik.

At least 19 recordsLinked to original sources

Ab initio electronic structure calculation of a new gene system using the negative factor counting method.

We report a calculation of the electronic structure (density of states and molecular orbitals) of a new gene system-the plasmid shuttle vector pCRR1-performed at the ab initio Hartree-Fock level. To deal with the aperiodicity of the biopolymer, a vectorized version of a negative factor counting (NFC) program has been implemented. With this efficient tool, DNA molecules of up to 100 deoxynucleotides (approximately 10,000 basis functions at the ab initio level) can be calculated routinely. In our calculation the base sequence of the plasmid is explicitly taken into account and a standard helical structure is assumed. Minimum as well as 6-31G basis sets are used in the calculation, and solvation effects are explicitly included. The calculation shows that solvation does not have a significant effect on the electronic structure of the biopolymer. It is found that the frontier orbitals (HOMO and LUMO) are highly localized on the bases. The interpretation of this result in terms of the frontier molecular orbital theory is that the attack of radiation-induced radicals is mainly on the base moieties.

Models, Genetic↗

Investigation of the possibility of solitary waves in the base stacks of DNA.

The possibility of the existence of solitary waves in DNA is investigated. On the basis of our classical model we do not find such a wave in a polynucleotide, but for a stack of adenine molecules without backbone we observe one. Possible extensions of the model for DNA are discussed. From our results we can conclude, that solitons exist in stacked systems without an additional backbone. At least the degree of freedom which couples a nucleotide base (pair) to the sugar-phosphate backbones (N-C stretching vibration) has to be treated with the help of the quantum equations of motion.

DNA↗

The effect of water and ions on the energy band structure of periodic alpha-helical polypeptides.

The solvent structure around several periodic polypeptides in the alpha-helical conformation has been determined by Monte-Carlo simulations. The calculations of the water clusters have been performed in the presence and absence of Na+ ions. The resulting hydration shell has been used to calculate the band structure of the polymers in the effective field of the water molecules and ions. The results show that the maximum change of the band widths and the band gaps is about 0.7 eV in the presence of the hydration shell. The band positions are shifted by up to 4.1 eV in the presence of water molecules and ions. The results have been compared with the band structure results of periodic polypeptides in the beta-pleated sheet conformation.

Ions↗

Quantum chemical calculations of model systems for ascorbic acid adducts with Schiff bases of lysine side chains: possibility of internal charge transfer in proteins.

Ab initio self-consistent field calculations for neutral and cationic ascorbic acid and model compounds have been performed. Furthermore, the bicyclic addition products of alpha-hydroxytetronic acid with methylglyoxal and with the Schiff base formed between methylglyoxal and methylamine have been calculated, again in their neutral and cationic forms, respectively. The results indicate that the investigated cations can act as strong electron acceptors. With the help of space-filling molecular models it has been demonstrated that such conformations of the Schiff base formed between the primary amino group of lysine side chains in proteins and the ascorbic acid methylglyoxal acetal are possible in which the lactone carbonyl group comes near to the N atoms of the peptide groups, so that charge can be transferred between these subunits.

Ascorbic Acid↗