000849925 001__ 849925
000849925 005__ 20240619083547.0
000849925 037__ $$aFZJ-2018-04021
000849925 041__ $$aEnglish
000849925 1001_ $$0P:(DE-Juel1)166572$$aNiether, Doreen$$b0$$eCorresponding author$$ufzj
000849925 1112_ $$aTwentieth Symposium on Thermophysical Properties$$cBoulder$$d2018-06-24 - 2018-06-29$$wUSA
000849925 245__ $$aUnravelling the hydrophobicity of urea in water using thermodiffusion: implications for protein denaturation
000849925 260__ $$c2018
000849925 3367_ $$033$$2EndNote$$aConference Paper
000849925 3367_ $$2DataCite$$aOther
000849925 3367_ $$2BibTeX$$aINPROCEEDINGS
000849925 3367_ $$2DRIVER$$aconferenceObject
000849925 3367_ $$2ORCID$$aLECTURE_SPEECH
000849925 3367_ $$0PUB:(DE-HGF)6$$2PUB:(DE-HGF)$$aConference Presentation$$bconf$$mconf$$s1544012544_1235$$xAfter Call
000849925 520__ $$aUrea is widely used as protein denaturant in aqueous solutions. Experiments and computer simulation studies have shown that it dissolves in water almost ideally at high concentrations, introducing little disruption in the water hydrogen bonded structure. However, at concentrations of the order of 5 M or higher, urea induces denaturation in a wide range of proteins. The origin of this behaviour is not completely understood, but it is believed to stem from a balance between urea-protein and urea-water interactions, with urea becoming possibly hydrophobic at a specific concentration range. The small changes observed in the water structure makes it difficult to connect the denaturation effects to solvation properties. Here we show that the exquisite sensitivity of thermodiffusion to solute-water interactions allows the identification of the onset of hydrophobicity of urea-water mixtures. The hydrophobic behaviour is reflected in a sign reversal of the temperature dependent slope of the Soret coefficient, which is observed, both in experiments and non-equilibrium computer simulations at approximately 5 M concentration of urea in water. This concentration regime corresponds to the one where abrupt changes in the denaturation of proteins are commonly observed. We show that the onset of hydrophobicity is intrinsically connected to the urea-water interactions. Our results allow us to identify correlations between the Soret coefficient and the partition coefficient, logP, hence establishing the thermodiffusion technique as a powerful approach to study hydrophobicity.
000849925 536__ $$0G:(DE-HGF)POF3-551$$a551 - Functional Macromolecules and Complexes (POF3-551)$$cPOF3-551$$fPOF III$$x0
000849925 7001_ $$0P:(DE-HGF)0$$aDi Lecce, Silvia$$b1
000849925 7001_ $$0P:(DE-HGF)0$$aBresme, Fernando$$b2
000849925 7001_ $$0P:(DE-Juel1)131034$$aWiegand, Simone$$b3$$ufzj
000849925 909CO $$ooai:juser.fz-juelich.de:849925$$pVDB
000849925 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)166572$$aForschungszentrum Jülich$$b0$$kFZJ
000849925 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)131034$$aForschungszentrum Jülich$$b3$$kFZJ
000849925 9131_ $$0G:(DE-HGF)POF3-551$$1G:(DE-HGF)POF3-550$$2G:(DE-HGF)POF3-500$$3G:(DE-HGF)POF3$$4G:(DE-HGF)POF$$aDE-HGF$$bKey Technologies$$lBioSoft – Fundamentals for future Technologies in the fields of Soft Matter and Life Sciences$$vFunctional Macromolecules and Complexes$$x0
000849925 9141_ $$y2018
000849925 920__ $$lyes
000849925 9201_ $$0I:(DE-Juel1)ICS-3-20110106$$kICS-3$$lWeiche Materie $$x0
000849925 980__ $$aconf
000849925 980__ $$aVDB
000849925 980__ $$aI:(DE-Juel1)ICS-3-20110106
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