Structural analysis and molecular modeling of the RvH2-e functional unit of Rapana venosa hemocyanin.
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.
Velkova
Ludmila
L
Institute of Organic Chemistry, Bulgarian Academy of Sciences, G. Bonchev 9, Sofia 1113, Bulgaria.
Dolashka
Pavlina
P
Dolashki
Aleksander
A
Voelter
Wolfgang
W
Atanasov
Boris
B
D000465:Algorithms; D000818:Animals; D002942:Circular Dichroism; D006433:Hemocyanins / Q000737:chemistry* / Q000302:isolation & purification; D006863:Hydrogen-Ion Concentration; D008956:Models, Chemical; D011489:Protein Denaturation; D017510:Protein Folding; D055550:Protein Stability; D021122:Protein Subunits / Q000737:chemistry; D012908:Snails / Q000378:metabolism*; D013696:Temperature; D013816:Thermodynamics
D021122:Protein Subunits; D006433:Hemocyanins