Effect of divalent metals on the molecular structure of protein: Modeling and spectroscopic approaches
Prof. Dr. Hanan Gouda Abdelwahab Ahmed Elhaes; Elkashef, Nahla M.; Abdel-Gawad, Fagr Kh; Shaban, Ahmad M.; Ibrahim, Medhat;
Abstract
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. © 2014 American Scientific Publishers.
Other data
| Title | Effect of divalent metals on the molecular structure of protein: Modeling and spectroscopic approaches | Authors | Prof. Dr. Hanan Gouda Abdelwahab Ahmed Elhaes ; Elkashef, Nahla M.; Abdel-Gawad, Fagr Kh; Shaban, Ahmad M.; Ibrahim, Medhat | Keywords | Fish;Protein;Molecular Modeling;HF;Heavy Metals;FTIR | Issue Date | 1-Apr-2014 | Publisher | AMER SCIENTIFIC PUBLISHERS | Journal | Journal of Computational and Theoretical Nanoscience | ISSN | 15461955 | DOI | 10.1166/jctn.2014.3465 | Scopus ID | 2-s2.0-84894644564 | Web of science ID | WOS:000332290400021 |
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