Structural analysis and molecular modeling of the RvH2-e functional unit of Rapana venosa hemocyanin
| Autor: | Wolfgang Voelter, Ludmila Velkova, Pavlina Dolashka, Aleksander Dolashki, Boris P. Atanasov |
|---|---|
| Rok vydání: | 2010 |
| Předmět: |
Protein Denaturation
Protein Folding Molecular model medicine.medical_treatment Snails Biophysics Biochemistry Analytical Chemistry medicine Animals Molecule Denaturation (biochemistry) Molecular Biology biology Protein Stability Chemistry Circular Dichroism Temperature Hemocyanin Hydrogen-Ion Concentration biology.organism_classification Circular dichroism spectra Protein Subunits Crystallography Rapana Models Chemical Hemocyanins Thermodynamics Algorithms |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1804:2177-2182 |
| ISSN: | 1570-9639 |
| DOI: | 10.1016/j.bbapap.2010.08.009 |
| Popis: | Rapana venosa hemocyanin (RvH), a circulating glycoprotein of the marine snail, has a complex structure. To provide details on the stability of the protein, one functional unit, RvH2-e, was compared with the native molecule and the structural subunits, RvH1 and RvH2, via pH–T diagrams, typical phase portraits for stability and denaturation reversibility. By analyzing the T transition curves of RvH2-e at different pH values, several parameters of the thermodynamic functions were obtained. Increasing the temperature from 25 °C to 55 °C, the reversibility of the molecule of protein also increases, opening a reversibility window within the range of pH 4.0–8.0. On analyzing the pH transition curves, the start of the acid denaturation (below pH 6) and alkaline denaturation (above pH 9) was determined to be between 20 °C and 35 °C. For this range, the thermodynamic functions ΔH° and ΔG° for a standard temperature of 25 °C were calculated. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect