Thermal Diffusion of Oligosaccharide Solutions: The Role of Chain Length and Structure

Blanco, Pablo M.; Kriegs, Hartmut; Arlt, Bastian; Wiegand, Simone

doi:10.1021/jp104534m

Cited by 29 publications

(34 citation statements)

References 41 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Likewise, Brenner's 41 kinematic model of thermal diffusion for liquid and gases establishes that D T is proportional to the thermal expansion coefficient. This linear correlation has also been observed for sugar solutions 42,43 and for alkanes in organic solvent. 44 12 We used the same symbols as in Fig.…”

Section: A Thermal Expansionsupporting

confidence: 70%

Peptide model systems: Correlation between thermophilicity and hydrophilicity

Niether

Kriegs

Dhont

et al. 2018

The Journal of Chemical Physics

Self Cite

View full text Add to dashboard Cite

In recent years, the response of biomolecules to a temperature gradient has been utilized to monitor reactions of biomolecules, but the underlying mechanism is not well understood due to the complexity of the multicomponent system. To identify some underlying principles, we investigate the thermal diffusion of small amide molecules in water systematically. We re-analyze previous measurements of urea and formamide and compare the results with acetamide, N-methylformamide, and N,N-dimethylformamide, amides with a lower hydrophilicity. It turns out that less hydrophilic substances do not show the typical temperature dependence of water soluble macromolecules. Analyzing temperature and concentration dependent measurements using an empirical expression originally derived for nonpolar mixtures, we find that the so-called isotope contribution depends strongly on the hydrophilicity of the solute. This can be qualitatively understood by comparing with molecular dynamic simulations of Lennard-Jones fluids. The hydrophobic/hydrophilic balance also influences the structure in the fluid and with that the thermal expansion coefficient, which correlates with the thermal diffusion coefficient. Furthermore, we observe a clear correlation of the temperature and concentration dependence of the Soret coefficient with the hydrophilicity, which can be quantitatively described by the partition coefficient log P.

show abstract

Section: A Thermal Expansionsupporting

confidence: 70%

Peptide model systems: Correlation between thermophilicity and hydrophilicity

Niether

Kriegs

Dhont

et al. 2018

The Journal of Chemical Physics

Self Cite

View full text Add to dashboard Cite

show abstract

“…Describing the chain length in terms of the persistence length l p , D T becomes constant when the chain length is of around two to three times l p . The chain length dependence of D T of alkanes 14 , polystyrene 23 , sugars 20 and also of glycols in aqueous solution 25 is already documented in literature. If we follow the argumentation of the simulation results we expect for glycols in ethanol a different behavior compared the aqueous solutions, because in contrast to water no hydration layer is formed.…”

Section: Introductionmentioning

confidence: 79%

“…Apart from low molecular weight mixtures also polymers solutions and colloidal suspensions in polar and non-polar solvents have been investigated [16][17][18] . For this study, the thermal expansion coefficient α and the kinematic viscosity ν are measured to compare to recent results on alkanes 15 and sugars 19,20 .…”

Section: Introductionmentioning

confidence: 99%

The Soret effect of mono-, di- and tri-glycols in ethanol

Klein

Wiegand

2011

Phys. Chem. Chem. Phys.

Self Cite

View full text Add to dashboard Cite

We employed thermal diffusion forced Rayleigh scattering (TDFRS) to investigate the chain length dependence of the thermal diffusion behavior of short glycols in ethanol. We studied three glycols, monoethylenglycol (MEG), diethylenglycol (DEG) and triethylenglycol (TEG), in an ethanol solution. In contrast to the polymer polyethylenglycol, the shorter glycols used within the framework of this study are completely soluble in ethanol, at least for low molar fractions. In order to guarantee a good solubility of the glycols, the measurements were limited to molar fractions of 10% and 20%. As the different glycols only differ by their chain length it will be possible to deduce its influence on the thermal diffusion properties. Due to the fairly short persistence length of the glycols, D(T) reaches already for the dimer a plateau value. This finding agrees with simulation results. Furthermore, the thermal expansion and the kinematic viscosity are measured to investigate if empirical correlations seen for other systems could be confirmed.

show abstract

“…This is probably a consequence of the difference in the ratio of thermal expansion coefficient α over viscosity η: the difference of the ratio between light and heavy water increases with increasing temperature [52,53]. Earlier studies have shown that the thermal diffusion coefficient is proportional to the ratio α/η [54,55]. This implies that the thermal diffusion coefficient becomes larger for systems which show a larger thermal expansion coefficient and which are less viscous.…”

Section: Influence Of D 2 Omentioning

confidence: 99%

Thermophoresis: The Case of Streptavidin and Biotin

et al. 2020

Self Cite

View full text Add to dashboard Cite

Thermophoretic behavior of a free protein changes upon ligand binding and gives access to information on the binding constants. The Soret effect has also been proven to be a promising tool to gain information on the hydration layer, as the temperature dependence of the thermodiffusion behavior is sensitive to solute–solvent interactions. In this work, we perform systematic thermophoretic measurements of the protein streptavidin (STV) and of the complex STV with biotin (B) using thermal diffusion forced Rayleigh scattering (TDFRS). Our experiments show that the temperature sensitivity of the Soret coefficient is reduced for the complex compared to the free protein. We discuss our data in comparison with recent quasi-elastic neutron scattering (QENS) measurements. As the QENS measurement has been performed in heavy water, we perform additional measurements in water/heavy water mixtures. Finally, we also elucidate the challenges arising from the quantiative thermophoretic study of complex multicomponent systems such as protein solutions.

show abstract

Thermal Diffusion of Oligosaccharide Solutions: The Role of Chain Length and Structure

Abstract: We investigated the chain length dependence of the thermodiffusion behavior of oligosaccharides by the infrared thermal diffusion forced Rayleigh scattering (IR-TDFRS)

Cited by 29 publications

References 41 publications

Peptide model systems: Correlation between thermophilicity and hydrophilicity

Peptide model systems: Correlation between thermophilicity and hydrophilicity

The Soret effect of mono-, di- and tri-glycols in ethanol

Thermophoresis: The Case of Streptavidin and Biotin

Contact Info

Product

Resources

About