Thermodynamic Analysis of Chitooligosaccharide Binding to Urtica dioica agglutinin by Isothermal Titration Calorimetry
Autor: | E. J. M. Van Damme, Willy J. Peumans, S. Katiyar, Avadhesha Surolia |
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Rok vydání: | 1999 |
Předmět: |
Enthalpy
Biophysics Oligosaccharides Chitin Calorimetry Chitobiose Biochemistry Magnoliopsida chemistry.chemical_compound Protein structure Lectins Binding site Molecular Biology Plant Proteins Binding Sites Chromatography Isothermal titration calorimetry Cell Biology Binding constant Protein Structure Tertiary Crystallography Monomer chemistry Thermodynamics Plant Lectins Antimicrobial Cationic Peptides |
Zdroj: | Bioscience Reports. 19:411-419 |
ISSN: | 1573-4935 0144-8463 |
Popis: | 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. |
Databáze: | OpenAIRE |
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