Effect of Divalent Metals on the Molecular Structure of Protein: Modeling and Spectroscopic Approaches
HF/3-21g** was used to study the possible interaction of Ca, Cd and Za with protein. Results indicate that each metal is attached with two hydrogen bondings in two hydrated protein chains. Protein structure has been affected as a result of interaction with the studied metals. The change
was noticed in the bond lengths and bond angle of the COOH group. The interaction decreases the calculated band gap energy and increases the total dipole moment which is a good indication for the reactivity of protein after interaction with the studied metals. FTIR verifies experimentally
the interaction and indicates that the characteristic bands of metal carboxylate are shifted 190∼200 cm–1 through the lower wavenumbers.
Keywords: FISH; FTIR; HEAVY METALS; HF; MOLECULAR MODELING; PROTEIN
Document Type: Research Article
Publication date: 01 April 2014
- Journal of Computational and Theoretical Nanoscience is an international peer-reviewed journal with a wide-ranging coverage, consolidates research activities in all aspects of computational and theoretical nanoscience into a single reference source. This journal offers scientists and engineers peer-reviewed research papers in all aspects of computational and theoretical nanoscience and nanotechnology in chemistry, physics, materials science, engineering and biology to publish original full papers and timely state-of-the-art reviews and short communications encompassing the fundamental and applied research.
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