scholarly journals Heparin binding domain peptides of antithrombin III: Analysis by isothermal titration calorimetry and circular dichroism spectroscopy

1994 ◽  
Vol 3 (4) ◽  
pp. 620-627 ◽  
Author(s):  
Ruth Tyler-Cross ◽  
Robert B. Harris ◽  
Michael Sobel ◽  
Dalila Marques
Keyword(s):  
Circular Dichroism ◽  
Isothermal Titration Calorimetry ◽  
Antithrombin Iii ◽  
Circular Dichroism Spectroscopy ◽  
Binding Domain ◽  
Titration Calorimetry ◽  
Heparin Binding ◽  
Heparin Binding Domain ◽  
Circular Dichroïsm

scholarly journals Thermodynamic Studies of Interactions between Sertraline Hydrochloride and Randomly Methylated β-Cyclodextrin Molecules Supported by Circular Dichroism Spectroscopy and Molecular Docking Results

2021 ◽  
Vol 22 (22) ◽  
pp. 12357
Author(s):  
Sylwia Belica-Pacha ◽  
Mateusz Daśko ◽  
Vyacheslav Buko ◽  
Ilya Zavodnik ◽  
Katarzyna Miłowska ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Circular Dichroism ◽  
Atmospheric Pressure ◽  
Association Constant ◽  
Circular Dichroism Spectroscopy ◽  
Titration Calorimetry ◽  
Computational Studies ◽  
K Value ◽  
Sertraline Hydrochloride ◽  
Circular Dichroïsm

The interaction between sertraline hydrochloride (SRT) and randomly methylated β-cyclodextrin (RMβCD) molecules have been investigated at 298.15 K under atmospheric pressure. The method used—Isothermal Titration Calorimetry (ITC) enabled to determine values of the thermodynamic functions like the enthalpy (ΔH), the entropy (ΔS) and the Gibbs free energy (ΔG) of binding for the examined system. Moreover, the stoichiometry coefficient of binding (n) and binding/association constant (K) value have been calculated from the experimental results. The obtained outcome was compared with the data from the literature for other non-ionic βCD derivatives interacting with SRT and the enthalpy-entropy compensation were observed and interpreted. Furthermore, the connection of RMβCD with SRT was characterized by circular dichroism spectroscopy (CD) and complexes of βCD derivatives with SRT were characterized through the computational studies with the use of molecular docking (MD).

scholarly journals Effects of freezing and the cryoprotectant lactobionic acid in the structure of GlnK protein evaluated by circular dichroism (CD) and isothermal titration calorimetry (ITC)

2016 ◽  
Vol 54 (1) ◽  
pp. 236-243 ◽  
Author(s):  
Cíntia Tiemi Misugi ◽  
Lizandra Kamradt Savi ◽  
Patrícia Kanczewski Iwankiw ◽  
Maria Lucia Masson ◽  
Marco Aurélio Schüler de Oliveira ◽  
...  
Keyword(s):  
Circular Dichroism ◽  
Isothermal Titration Calorimetry ◽  
Titration Calorimetry ◽  
Lactobionic Acid ◽  
Circular Dichroïsm
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