A thermodynamic study of nickel ion interaction with bovine carbonic anhydrase II molecule

Behbehani, G. Rezaei; Saboury, Ali Akbar; Yahaghi, E.

doi:10.1007/s10973-009-0012-9

Cited by 4 publications

(3 citation statements)

References 23 publications

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“…Protein interactions with small ligands (including co‐factors and drugs) Protein/peptide interactions with metals and ions Protein/peptide interactions with nucleic acids …”

Section: Introductionmentioning

confidence: 99%

Applications of isothermal titration calorimetry in pure and applied research—survey of the literature from 2010

Ghai

Falconer

Collins

2011

J of Molecular Recognition

167

108

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Isothermal titration calorimetry (ITC) is a biophysical technique for measuring the formation and dissociation of molecular complexes and has become an invaluable tool in many branches of science from cell biology to food chemistry. By measuring the heat absorbed or released during bond formation, ITC provides accurate, rapid, and label-free measurement of the thermodynamics of molecular interactions. In this review, we survey the recent literature reporting the use of ITC and have highlighted a number of interesting studies that provide a flavour of the diverse systems to which ITC can be applied. These include measurements of protein-protein and protein-membrane interactions required for macromolecular assembly, analysis of enzyme kinetics, experimental validation of molecular dynamics simulations, and even in manufacturing applications such as food science. Some highlights include studies of the biological complex formed by Staphylococcus aureus enterotoxin C3 and the murine T-cell receptor, the mechanism of membrane association of the Parkinson's disease-associated protein α-synuclein, and the role of non-specific tannin-protein interactions in the quality of different beverages. Recent developments in automation are overcoming limitations on throughput imposed by previous manual procedures and promise to greatly extend usefulness of ITC in the future. We also attempt to impart some practical advice for getting the most out of ITC data for those researchers less familiar with the method.

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“…Protein interactions with small ligands (including co‐factors and drugs) Protein/peptide interactions with metals and ions Protein/peptide interactions with nucleic acids …”

Section: Introductionmentioning

confidence: 99%

Applications of isothermal titration calorimetry in pure and applied research—survey of the literature from 2010

Ghai

Falconer

Collins

2011

J of Molecular Recognition

167

108

View full text Add to dashboard Cite

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“…We have shown previously that the heats of the ligand + HSA interactions in the aqueous solvent mixtures, can be calculated via the following equation [9][10][11][12][13][14]:…”

Section: Resultsmentioning

confidence: 99%

A Comparative Study on the Interaction of Sulfonamide and Nanosulfonamide with Human Serum Albumin

Behbehani

Sadr

Nabipur

et al. 2013

Journal of Chemistry

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Binding parameters of the N-phenyl benzene sulfonyl hydrazide, sulfonamide, and nanosulfonamide interaction with human serum albumin were determined by calorimetry method. The obtained binding parameters indicated that sulfonamide in the second binding sites has higher affinity for binding than the first binding sites. The binding process of sulfonamide to HSA is both enthalpy and entropy driven. The associated equilibrium constants confirm that sulfonamide binds to HSA with high affinity (2.2×106and 3.86105 M−1for first and second sets of binding sites, resp.). The obtained results indicate that sulfonamide increases the HSA antioxidant property. Nanosulfonamide has much more affinity for HSA (3.6×106 M−1) than sulfonamide.

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“…We have shown previously that the heats of the ligand ? JBU interactions in the aqueous solvent mixtures can be calculated via the following equation [7][8][9][10][11][12]:…”

Section: Resultsmentioning

confidence: 99%

The Interaction of Ferric Ions with Jack Bean Urease by Isothermal Titration Calorimetry

Behbehani

Barzegar

2013

Natl. Acad. Sci. Lett.

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The aim of the investigations was to measure the influence of Fe 3? ion on jack bean urease (JBU) activity. Interaction between Fe 3? and JBU, is examined using isothermal titration calorimetry. It was found that Fe 3? ions acted as a non-cooperative inhibitor of JBU, and there is a set of 12 identical and independent binding sites for Fe 3? ions. The small structural parameters show that there are little changes on the JBU structure, indicating that Fe 3? has minor effect on the JBU activity. The association equilibrium constant is 42,484.13 ± 110 mol l-1 , indicating the moderate interaction of Fe 3? ion with JBU. The molar enthalpy of binding is DH =-4.33 kJ mol-1 .

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A thermodynamic study of nickel ion interaction with bovine carbonic anhydrase II molecule

Cited by 4 publications

References 23 publications

Applications of isothermal titration calorimetry in pure and applied research—survey of the literature from 2010

Applications of isothermal titration calorimetry in pure and applied research—survey of the literature from 2010

A Comparative Study on the Interaction of Sulfonamide and Nanosulfonamide with Human Serum Albumin

The Interaction of Ferric Ions with Jack Bean Urease by Isothermal Titration Calorimetry

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