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• W2070372406 abstract "An impact of 0.5 to 3 M choline dihydrogen phosphate, [ch][dhp], the biotechnologically relevant ionic substance, on the thermal stability of a model globular protein, α-chymotrypsin (α-CT), has been studied exploiting the highly sensitive differential scanning calorimetry (DSC) technique. The notable overall stabilizing effect of <mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML id=M1><mml:mn>11</mml:mn><mml:mo>±</mml:mo><mml:mn>2</mml:mn></mml:math> K regarding the thermal transition (melting) temperature, <mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML id=M2><mml:mrow><mml:msub><mml:mrow><mml:mi>T</mml:mi></mml:mrow><mml:mrow><mml:mi>m</mml:mi></mml:mrow></mml:msub></mml:mrow></mml:math>, has been detected. For this kind of series, for the first time, the calorimetric melting enthalpy <mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML id=M3><mml:mo stretchy=false>(</mml:mo><mml:mi mathvariant=normal>Δ</mml:mi><mml:msub><mml:mrow><mml:mi>H</mml:mi></mml:mrow><mml:mrow><mml:mtext>cal</mml:mtext></mml:mrow></mml:msub><mml:mi> </mml:mi><mml:mo stretchy=false>)</mml:mo></mml:math> and transition entropy <mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML id=M4><mml:mo stretchy=false>(</mml:mo><mml:mi mathvariant=normal>Δ</mml:mi><mml:msub><mml:mrow><mml:mi>S</mml:mi></mml:mrow><mml:mrow><mml:mi>m</mml:mi></mml:mrow></mml:msub><mml:mo stretchy=false>)</mml:mo></mml:math> parameters have been determined simultaneously throughout. The first analysis indicated a two-phase impact implying (a) the initial, dramatic drop in both <mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML id=M5><mml:mi mathvariant=normal>Δ</mml:mi><mml:msub><mml:mrow><mml:mi>H</mml:mi></mml:mrow><mml:mrow><mml:mtext>cal</mml:mtext></mml:mrow></mml:msub><mml:mi> </mml:mi></mml:math> and <mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML id=M6><mml:mi mathvariant=normal>Δ</mml:mi><mml:msub><mml:mrow><mml:mi>S</mml:mi></mml:mrow><mml:mrow><mml:mi>m</mml:mi></mml:mrow></mml:msub></mml:math>, obviously connected to specific, direct interaction between the [ch][dhp] components and α-CT’s charged groups (within 0 to 1 mol/L [ch][dhp]), leading to the essential rearrangement of the interfacial hydrogen-bonded (HB) network; and (b) the follow-up (within 1 to 3.0 mol/L [ch][dhp]), modest changes in <mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML id=M7><mml:mi mathvariant=normal>Δ</mml:mi><mml:msub><mml:mrow><mml:mi>H</mml:mi></mml:mrow><mml:mrow><mml:mtext>cal</mml:mtext></mml:mrow></mml:msub><mml:mi> </mml:mi></mml:math> and lack of changes in <mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML id=M8><mml:mi mathvariant=normal>Δ</mml:mi><mml:msub><mml:mrow><mml:mi>S</mml:mi></mml:mrow><mml:mrow><mml:mi>m</mml:mi></mml:mrow></mml:msub></mml:math>, seemingly connected with a subsequent steady strengthening of already reformed HB network, respectively. These changes, presumably, are primarily facilitated by Coulombic interactions between the [dhp] anions and solvent-exposed positively charged amino groups of α-CT." @default.
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• W2070372406 date "2014-09-07" @default.
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• W2070372406 title "Notable Stabilization of <i>α</i>-Chymotrypsin by the Protic Ionic Additive, [ch][dhp]: Calorimetric Evidence for a Fine Enthalpy/Entropy Balance" @default.
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• W2070372406 doi "https://doi.org/10.1155/2014/834189" @default.
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