Calcium-induced calmodulin conformational change. Electrochemical evaluation
Autor: | Isabel P.G. Fernandes, Ana Maria Oliveira-Brett |
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Rok vydání: | 2017 |
Předmět: |
Models
Molecular Protein Denaturation Conformational change Time Factors Calmodulin Biophysics chemistry.chemical_element 02 engineering and technology Calcium 010402 general chemistry Electrochemistry 01 natural sciences Animals Physical and Theoretical Chemistry Tyrosine Protein Structure Quaternary Electrodes Dose-Response Relationship Drug biology Chemistry General Medicine Hydrogen-Ion Concentration 021001 nanoscience & nanotechnology biology.organism_classification Carbon 0104 chemical sciences Dielectric spectroscopy Biochemistry biology.protein Cattle Eukaryote Differential pulse voltammetry 0210 nano-technology Oxidation-Reduction |
Zdroj: | Bioelectrochemistry. 113:69-78 |
ISSN: | 1567-5394 |
Popis: | Calmodulin (CaM) is an essential protein present in all eukaryote cells, ranging from vertebrates to unicellular organisms. CaM is the most important Ca 2 + signalling protein, composed of two domains, N- and C-terminal domains, linked by a flexible central α-helix, and is responsible for the regulation of numerous calcium-mediated signalling pathways. Four calcium ions bind to CaM, changing its conformation and determining how it recognizes and regulates its cellular targets. The oxidation mechanism of native and denatured CaM, at a glassy carbon electrode, was investigated using differential pulse voltammetry and electrochemical impedance spectroscopy. Native and denatured CaM presented only one oxidation peak, related to the tyrosine amino acid residue oxidation. Calcium-induced calmodulin conformational change and the influence of Ca 2 + concentration on the electrochemical behaviour of CaM were evaluated, and significant differences, in the tyrosine amino acid residue peak potential and current, in the absence and in the presence of calcium ions, were observed. Gravimetric measurements were performed with a graphite coated piezoelectric quartz crystal with adsorbed CaM, and calcium aggregation by CaM was demonstrated. |
Databáze: | OpenAIRE |
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