caa a22 4500 463192400 CHVBK 20180406164913.0 cr unu---uuuuu 170326e20070101xx s 000 0 eng 10.1007/s10973-006-7843-4 doi (NATIONALLICENCE)springer-10.1007/s10973-006-7843-4 Thermodynamicstudy of the thermal denaturation of a globular protein in the presence ofdifferent ligands [Elektronische Daten] [Elena Blanco, J. Ruso, J. Sabín, G. Prieto, F. Sarmiento] By means of difference UV-Vis spectra, the thermal denaturation of catalase has been studied in the presence of different surfactants: sodium perfluorooctanoate, sodium octanoate and sodium dodecanoate. These results indicate that hydrogenated surfactants play two opposite roles in the folding and stability of catalase, they act as a structure stabiliser at a low molar concentrations (enhancing T m) and as a destabilizer at a higher concentrations (diminishing T m). Meanwhile sodium perfluorooctanoate enhances T m in the whole concentration range. An approach for the determination of the heat capacity, enthalpy and entropy has been made, finding that for the three studied surfactants, at all concentrations, the enthalpy term dominates the entropy term. Springer-Verlag, 2007 catalase nationallicence ligands nationallicence thermal unfolding nationallicence thermodynamics nationallicence Blanco Elena Group of Biophysics and Interfaces, Department of Applied Physics, Faculty of Physics, University of Santiago de Compostela, 15782, Santiago de Compostela, Spain aut Ruso J. Group of Biophysics and Interfaces, Department of Applied Physics, Faculty of Physics, University of Santiago de Compostela, 15782, Santiago de Compostela, Spain aut Sabín J. Group of Biophysics and Interfaces, Department of Applied Physics, Faculty of Physics, University of Santiago de Compostela, 15782, Santiago de Compostela, Spain aut Prieto G. Group of Biophysics and Interfaces, Department of Applied Physics, Faculty of Physics, University of Santiago de Compostela, 15782, Santiago de Compostela, Spain aut Sarmiento F. Group of Biophysics and Interfaces, Department of Applied Physics, Faculty of Physics, University of Santiago de Compostela, 15782, Santiago de Compostela, Spain aut Journal of Thermal Analysis and Calorimetry Kluwer Academic Publishers 87/1(2007-01-01), 143-147 1388-6150 87:1<143 2007 87 10973 https://doi.org/10.1007/s10973-006-7843-4 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10973-006-7843-4 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Blanco Elena Group of Biophysics and Interfaces, Department of Applied Physics, Faculty of Physics, University of Santiago de Compostela, 15782, Santiago de Compostela, Spain aut NATIONALLICENCE 700 1- Ruso J. Group of Biophysics and Interfaces, Department of Applied Physics, Faculty of Physics, University of Santiago de Compostela, 15782, Santiago de Compostela, Spain aut NATIONALLICENCE 700 1- Sabín J. Group of Biophysics and Interfaces, Department of Applied Physics, Faculty of Physics, University of Santiago de Compostela, 15782, Santiago de Compostela, Spain aut NATIONALLICENCE 700 1- Prieto G. Group of Biophysics and Interfaces, Department of Applied Physics, Faculty of Physics, University of Santiago de Compostela, 15782, Santiago de Compostela, Spain aut NATIONALLICENCE 700 1- Sarmiento F. Group of Biophysics and Interfaces, Department of Applied Physics, Faculty of Physics, University of Santiago de Compostela, 15782, Santiago de Compostela, Spain aut NATIONALLICENCE 773 0- Journal of Thermal Analysis and Calorimetry Kluwer Academic Publishers 87/1(2007-01-01), 143-147 1388-6150 87:1<143 2007 87 10973 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer