scholarly journals Isothermal Titration Calorimetry: Thermodynamic Analysis of the Binding Thermograms of Molecular Recognition Events by Using Equilibrium Models

10.5772/53311 ◽  
2013 ◽  
Author(s):  
Jose C. ◽  
Javier Murciano-Calles ◽  
Eva S. ◽  
Manuel Iglesias-Bexiga ◽  
Irene Luque ◽  
...  
Keyword(s):  
Molecular Recognition ◽  
Isothermal Titration Calorimetry ◽  
Thermodynamic Analysis ◽  
Titration Calorimetry ◽  
Equilibrium Models

Thermodynamic analysis of binding and protonation in DOTAP/DOPE (1:1): DNA complexes using isothermal titration calorimetry

2003 ◽  
Vol 104 (1) ◽  
pp. 67-78 ◽  
Author(s):  
Brian A. Lobo ◽  
Gary S. Koe ◽  
Janet G. Koe ◽  
C.Russell Middaugh
Keyword(s):  
Isothermal Titration Calorimetry ◽  
Thermodynamic Analysis ◽  
Titration Calorimetry ◽  
Dna Complexes

Thermodynamic analysis of binding between drugs and glycosaminoglycans by isothermal titration calorimetry and fluorescence spectroscopy

2007 ◽  
Vol 32 (2) ◽  
pp. 105-114 ◽  
Author(s):  
Hélder A. Santos ◽  
José A. Manzanares ◽  
Lasse Murtomäki ◽  
Kyösti Kontturi
Keyword(s):  
Fluorescence Spectroscopy ◽  
Isothermal Titration Calorimetry ◽  
Thermodynamic Analysis ◽  
Titration Calorimetry

Thermodynamic analysis of polyphenols retention in polymer resin chromatography by van’t Hoff plot and isothermal titration calorimetry

2019 ◽  
Vol 1608 ◽  
pp. 460405 ◽  
Author(s):  
Joao C. Simoes-Cardoso ◽  
Noriko Yoshimoto ◽  
Shuichi Yamamoto
Keyword(s):  
Isothermal Titration Calorimetry ◽  
Thermodynamic Analysis ◽  
Titration Calorimetry ◽  
Polymer Resin ◽  
Hoff Plot

Thermodynamic Analysis of Chitooligosaccharide Binding to Urtica dioica agglutinin by Isothermal Titration Calorimetry

1999 ◽  
Vol 19 (5) ◽  
pp. 411-419 ◽  
Author(s):  
Samiksha Katiyar ◽  
E. J. M. Van Damme ◽  
Willy J. Peumans ◽  
Avadhesha Surolia
Keyword(s):  
Thermodynamic Parameters ◽  
Isothermal Titration Calorimetry ◽  
Thermodynamic Analysis ◽  
Binding Constant ◽  
Urtica Dioica ◽  
Titration Calorimetry ◽  
Sugar Residue ◽  
Binding Enthalpy ◽  
Urtica Dioica Agglutinin

UDA (Urtica dioica agglutinin) contains two hevein like domains with two non-identical interacting sites and is specific for chitooligosaccharides. The binding of chitooligosaccharides to UDA was studied by Isothermal Titration Calorimetry. Each site is composed of three subsites, each binding to a sugar residue. Thermodynamic parameters obtained show that while chitobiose has two independent non-interacting sites, chitotriose, chitotetrose and chitopentose have two interacting sites on each monomer of UDA. Values of binding enthalpy (ΔH) increase almost by a factor of 7 in going from chitobiose to chitotriose indicating the existence of three subsites in the combining site of UDA. The binding constant for chitotetrose and chitopentose increase without any further enhancement in the values of ΔH indicating that for oligomers larger than chitotriose interaction is favoured entropically.

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