Calorimeters for biotechnology

Russell, Donald J.; Hansen, Lee D.

doi:10.1016/j.tca.2005.08.023

Cited by 18 publications

(11 citation statements)

References 40 publications

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“…The CSC isothermal titration calorimeter has 1 mL fixed conical cells and a fast response time. 4 The prototypal heat conduction microcalorimeter, also called heat-leak, heat-flow or heat-flux calorimeter, developed by Suurkuusk and Wadsö, is described in reference 5. In a heat conduction microcalorimeter, heat released (or taken up) in the reaction vessel flows to (or from) a surrounding heat sink, usually an aluminum block.…”

Section: Introductionmentioning

confidence: 99%

On the use of titration calorimetry to study the association of surfactants in aqueous solutions

Olofsson¹,

Loh²

2009

J. Braz. Chem. Soc.

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Section: Introductionmentioning

confidence: 99%

On the use of titration calorimetry to study the association of surfactants in aqueous solutions

Olofsson¹,

Loh²

2009

J. Braz. Chem. Soc.

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“…Isothermal titration calorimetry (ITC) is a sensitive technique that directly determines the thermodynamic parameters of protein-protein or protein-ligand interactions (15). ITC dilution experiments have been used to investigate the monomer-dimer and monomer-heptamer equilibrium and micellar assembly of antibiotic protein, lipids, and surfactants (16)(17)(18)(19)(20).…”

Section: Introductionmentioning

confidence: 99%

The Role of Secondary Structure in the Entropically Driven Amelogenin Self-Assembly

Lakshminarayanan

Fan

et al. 2007

Biophysical Journal

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Amelogenin, the major extracellular enamel matrix protein, plays critical roles in controlling enamel mineralization. This generally hydrophobic protein self-assembles to form nanosphere structures under certain solution conditions. To gain clearer insight into the mechanisms of amelogenin self-assembly, we first investigated the occurrences of secondary structures within its sequence. By applying isothermal titration calorimetry (ITC), we determined the thermodynamic parameters associated with protein-protein interactions and with conformational changes during self-assembly. The recombinant porcine full length (rP172) and a truncated amelogenin lacking the hydrophilic C-terminal (rP148) were used. Circular dichroism (CD) measurements performed at low concentrations (<5 microM) revealed the presence of the polyproline-type II (PPII) conformation in both amelogenins in addition to alpha-helix and unordered conformations. Structural transition from PPII/unordered to beta-sheet was observed for both proteins at higher concentrations (>62.5 microM) and upon self-assembly. ITC measurements indicated that the self-assembly of rP172 and rP148 is entropically driven (+DeltaS(A)) and energetically favorable (-DeltaG(A)). The magnitude of enthalpy (DeltaH(A)) and entropy changes of assembly (DeltaS(A)) were smaller for rP148 than rP172, whereas the Gibbs free energy change of assembly (DeltaG(A)) was not significantly different. It was found that rP172 had higher PPII content than rP148, and the monomer-multimer equilibrium for rP172 was observed in a narrower protein concentration range when compared to rP148. The large positive enthalpy and entropy changes in both cases are attributed to the release of ordered water molecules and the associated entropy gain (due to the hydrophobic effect). These findings suggest that PPII conformation plays an important role in amelogenin self-assembly and that rP172 assembly is more favorable than rP148. The data are direct evidence for the notion that hydrophobic interactions are the main driving force for amelogenin self-assembly.

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“…the number of binding sites) are easily calculated from the titration curve. When a reaction is substantially incomplete, K a as well as DH and the stoichiometry can be calculated from the calorimetric titration curve if the total concentration of reactant in the reaction vessel, [M] T , is chosen so that 10 \ K a [M] T \ 1000 [23][24][25][26]. K a values in the range 10 2 -10 9 can be estimated with this method.…”

Section: Thermodynamics Of Non-covalent Binding Reactionsmentioning

confidence: 99%

“…The model equations used to fit the data are for a 1:1 binding as given in Ref. [24] except that DT was substituted for Q…”

Section: Thermodynamics Of Non-covalent Binding Reactionsmentioning

confidence: 99%

From Biochemistry to Physiology: The Calorimetry Connection

Hansen

Russell²,

Choma³

2007

Cell Biochem Biophys

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This article provides guidelines for selecting optimal calorimetric instrumentation for applications in biochemistry and biophysics. Applications include determining thermodynamics of interactions in non-covalently bonded structures, and determining function through measurements of enzyme kinetics and metabolic rates. Specific examples illustrating current capabilities and methods in biological calorimetry are provided. Commercially available calorimeters are categorized by application and by instrument characteristics (isothermal or temperature-scanning, reaction vessel volume, heat rate detection limit, fixed or removable reaction vessels, etc.). Advantages and limitations of commercially available calorimeters are listed for each application in biochemistry, biophysics, and physiology.

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Calorimeters for biotechnology

Cited by 18 publications

References 40 publications

On the use of titration calorimetry to study the association of surfactants in aqueous solutions

On the use of titration calorimetry to study the association of surfactants in aqueous solutions

The Role of Secondary Structure in the Entropically Driven Amelogenin Self-Assembly

From Biochemistry to Physiology: The Calorimetry Connection

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