scholarly journals Using Isothermal Titration Calorimetry to Determine Thermodynamic Parameters of Protein–Glycosaminoglycan Interactions

2014 ◽  
pp. 315-324 ◽  
Author(s):  
Amit K. Dutta ◽  
Jörg Rösgen ◽  
Krishna Rajarathnam
Keyword(s):  
Thermodynamic Parameters ◽  
Isothermal Titration Calorimetry ◽  
Titration Calorimetry

scholarly journals Calorimetric techniques applied to the thermodynamic study of interactions between proteins and polysaccharides

2016 ◽  
Vol 46 (8) ◽  
pp. 1491-1497
Author(s):  
Monique Barreto Santos ◽  
Bernardo de Sá Costa ◽  
Edwin Elard Garcia Rojas
Keyword(s):  
Differential Scanning Calorimetry ◽  
Thermodynamic Parameters ◽  
Isothermal Titration Calorimetry ◽  
Thermal Energy ◽  
Titration Calorimetry ◽  
Biological Macromolecules ◽  
Valuable Insight ◽  
Scanning Calorimetry ◽  
Temperature Scanning ◽  
Insight Into

ABSTRACT: The interactions between biological macromolecules have been important for biotechnology, but further understanding is needed to maximize the utility of these interactions. Calorimetric techniques provide information regarding these interactions through the thermal energy that is produced or consumed during interactions. Notable techniques include differential scanning calorimetry, which generates a thermodynamic profile from temperature scanning, and isothermal titration calorimetry that provide the thermodynamic parameters directly related to the interaction. This review described how calorimetric techniques can be used to study interactions between proteins and polysaccharides, and provided valuable insight into the thermodynamics of their interaction.

Thermodynamic parameters of anion binding to halorhodopsin from Natronomonas pharaonis by isothermal titration calorimetry

2013 ◽  
Vol 172 ◽  
pp. 61-67 ◽  
Author(s):  
Saori Hayashi ◽  
Jun Tamogami ◽  
Takashi Kikukawa ◽  
Haruka Okamoto ◽  
Kazumi Shimono ◽  
...  
Keyword(s):  
Thermodynamic Parameters ◽  
Isothermal Titration Calorimetry ◽  
Anion Binding ◽  
Titration Calorimetry ◽  
Natronomonas Pharaonis

scholarly journals Polarizability and isotope effects on dispersion interactions in water

2019 ◽  
Vol 2 (1) ◽  
Author(s):  
Yi-Yang Zhan ◽  
Qi-Chun Jiang ◽  
Kentaro Ishii ◽  
Takuya Koide ◽  
Osamu Kobayashi ◽  
...  
Keyword(s):  
Interaction Energy ◽  
Thermodynamic Parameters ◽  
Isotope Effect ◽  
Isothermal Titration Calorimetry ◽  
Isotope Effects ◽  
Hydrophobic Effect ◽  
Dispersion Interaction ◽  
Titration Calorimetry ◽  
Dispersion Interactions ◽  
Precise Evaluation

AbstractTrue understanding of dispersion interaction in solution remains elusive because of difficulty in the precise evaluation of its interaction energy. Here, the effect of substituents with different polarizability on dispersion interactions in water is discussed based on the thermodynamic parameters determined by isothermal titration calorimetry for the formation of discrete aggregates from gear-shaped amphiphiles (GSAs). The substituents with higher polarizability enthalpically more stabilize the nanocube, which is due to stronger dispersion interactions and to the hydrophobic effect. The differences in the thermodynamic parameters for the nanocubes from the GSAs with CH3 and CD3 groups are also discussed to lead to the conclusion that the H/D isotope effect on dispersion interactions is negligibly small, which is due to almost perfect entropy-enthalpy compensation between the two isotopomers.

scholarly journals Isothermal titration calorimetry as a complementary method for investigating nanoparticle–protein interactions

Nanoscale ◽  
2019 ◽  
Vol 11 (41) ◽  
pp. 19265-19273 ◽  
Author(s):  
Domenik Prozeller ◽  
Svenja Morsbach ◽  
Katharina Landfester
Keyword(s):  
Protein Adsorption ◽  
Thermodynamic Parameters ◽  
Intermolecular Interactions ◽  
Isothermal Titration Calorimetry ◽  
Protein Interactions ◽  
Titration Calorimetry ◽  
Complementary Technique ◽  
Complementary Method

Isothermal titration calorimetry (ITC) is a complementary technique that can be used for investigations of protein adsorption on nanomaterials, as it quantifies the thermodynamic parameters of intermolecular interactionsin situ.

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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