2016
DOI: 10.1021/acs.biochem.6b00431
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Abstract: We report differential scanning calorimetry (DSC) experiments between 10 and 120 °C of Dengue 4 envelope protein domain 3 (DEN4 ED3), a small 107-residue monomeric globular protein domain. The thermal unfolding of DEN4 ED3 was fully reversible and exhibited two peculiar endothermic peaks. AUC (analytical ultracentrifugation) experiments at 25 °C indicated that DEN4 ED3 was monomeric. Detailed thermodynamic analysis indicated that the two endothermic peaks separated with an increasing protein concentration, and… Show more

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Cited by 19 publications
(24 citation statements)
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“…Although current technologies do not allow the determination of the interaction energies at atomic level, the systematic comparison of the thermodynamic data and the high-resolution crystal structures strongly suggest that improved local packing (including stronger van der Waals interactions) and improved hydration structures are the two main factors driving enthalpy-driven thermal stabilization. This is the first report to show that the replacement of a surface residue with a bulky hydrophobic residue (i.e., Ile 38 with fraction ASA of 0.66 AE 0.07) can stabilize a globular protein, which is in sharp contrast to the well-accepted theory that a hydrophobic residue on a protein surface is destabilizing or may drive aggregation [22,30]. From a practical perspective, our observations may provide a novel and generic strategy for thermally stabilizing proteins in an enthalpy-driven way by the judicious placement of hydrophobic residues on their molecular surfaces.…”
Section: Resultscontrasting
confidence: 71%
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“…Although current technologies do not allow the determination of the interaction energies at atomic level, the systematic comparison of the thermodynamic data and the high-resolution crystal structures strongly suggest that improved local packing (including stronger van der Waals interactions) and improved hydration structures are the two main factors driving enthalpy-driven thermal stabilization. This is the first report to show that the replacement of a surface residue with a bulky hydrophobic residue (i.e., Ile 38 with fraction ASA of 0.66 AE 0.07) can stabilize a globular protein, which is in sharp contrast to the well-accepted theory that a hydrophobic residue on a protein surface is destabilizing or may drive aggregation [22,30]. From a practical perspective, our observations may provide a novel and generic strategy for thermally stabilizing proteins in an enthalpy-driven way by the judicious placement of hydrophobic residues on their molecular surfaces.…”
Section: Resultscontrasting
confidence: 71%
“…The ratio between Van't Hoff (DH VH ) and the calorimetric enthalpy (DH cal ) was equal to 1.0 indicating that no intermolecular interactions, aggregation and/or intermediates appeared under the DSC measurement condition ( Table 1; Fig. S2) [21,22]. The melting temperatures (T m ) of the variants with Gly 14 , Ala 14 , or Val 14 increased by 7.68 to 16.18, À1.96 to 5.19, or 0.66 to 11.09°C, respectively (Table 1; Fig.…”
Section: Thermodynamics Of Bpti Variantsmentioning
confidence: 99%
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“…DSC measurements were performed using a VP-DSC MicroCalorimeter (Microcal, MA, USA) at a scan rate of 1.0 °C/min in the temperature range of 5 to 90 °C. The individual apparent heat capacity curves were analyzed with a two-state model using a non-linear least-square fitting method and by assuming a linear temperature dependence of the heat capacity for the native and denatured states212223 (Fig. 1).…”
Section: Methodsmentioning
confidence: 99%
“…Recently, a few single-domain globular proteins (CheY [21], Cro repressor [22], PSD95-PDZ3 [23][24], and DEN4 ED3 [25]) exhibiting DSC thermograms with two endothermic peaks have been reported. Surprisingly, the thermal denaturation is reversible, and the proteins are monomeric both in the native and denatured states, indicating that aggregation was not the reason for the unexpected observation nor for the MG state, which usually appears only under extreme conditions.…”
Section: Introductionmentioning
confidence: 99%