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Izvorni znanstveni članak
Thermal Perturbation of the Equilibrium System Ribonuclease A-Cytidine 3'-Monophosphate at pR 5.5
Mirna Flogel
; Department of Medical Biochemistry, Faculty of Pharmacy and Biochemistry, University of Zagreb, Zagreb
Tihana Žanić
; Department of Medical Biochemistry, Faculty of Pharmacy and Biochemistry, University of Zagreb, Zagreb
| Puni tekst: engleski, pdf (3 MB) | str. 99-105 | citiraj | |
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APA 6th Edition Flogel, M. i Žanić, T. (1985). Thermal Perturbation of the Equilibrium System Ribonuclease A-Cytidine 3'-Monophosphate at pR 5.5. Croatica Chemica Acta, 58 (1), 99-105. Preuzeto s https://hrcak.srce.hr/177745 MLA 8th Edition Flogel, Mirna i Tihana Žanić. "Thermal Perturbation of the Equilibrium System Ribonuclease A-Cytidine 3'-Monophosphate at pR 5.5." Croatica Chemica Acta, vol. 58, br. 1, 1985, str. 99-105. https://hrcak.srce.hr/177745. Citirano 06.03.2021. Chicago 17th Edition Flogel, Mirna i Tihana Žanić. "Thermal Perturbation of the Equilibrium System Ribonuclease A-Cytidine 3'-Monophosphate at pR 5.5." Croatica Chemica Acta 58, br. 1 (1985): 99-105. https://hrcak.srce.hr/177745 Harvard Flogel, M., i Žanić, T. (1985). 'Thermal Perturbation of the Equilibrium System Ribonuclease A-Cytidine 3'-Monophosphate at pR 5.5', Croatica Chemica Acta, 58(1), str. 99-105. Preuzeto s: https://hrcak.srce.hr/177745 (Datum pristupa: 06.03.2021.) Vancouver Flogel M, Žanić T. Thermal Perturbation of the Equilibrium System Ribonuclease A-Cytidine 3'-Monophosphate at pR 5.5. Croatica Chemica Acta [Internet]. 1985 [pristupljeno 06.03.2021.];58(1):99-105. Dostupno na: https://hrcak.srce.hr/177745 IEEE M. Flogel i T. Žanić, "Thermal Perturbation of the Equilibrium System Ribonuclease A-Cytidine 3'-Monophosphate at pR 5.5", Croatica Chemica Acta, vol.58, br. 1, str. 99-105, 1985. [Online]. Dostupno na: https://hrcak.srce.hr/177745. [Citirano: 06.03.2021.] |
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Sažetak
The equilibrium system ribonuclease A-cytidine 3'-monophosphate
at pH 5.5, was submitted to thermal perturbation. A derivative
fractional degree of saturation with respect to a temperature raise of twenty degrees was recorded as a function of free ligand concentration. The analysis of the thermal perturbation curve directly yields L1HO and L1GO of the binding reaction. The evaluated thermodynamic parameters are in good agreement with the values obtained by other methods. The thermal perturbation technique proved to be an elegant, time and material saving experimental method in providing accurate thermodynamic information about ligand-macromolecule interactions.
Hrčak ID: 177745
URI
https://hrcak.srce.hr/177745
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