Thermophoresis as a probe of particle–solvent interactions: The case of protein solutions

2004 ◽  
Vol 6 (7) ◽  
pp. 1616-1622 ◽  
Author(s):  
Roberto Piazza ◽  
Sara Iacopini ◽  
Benedetta Triulzi
Keyword(s):  
Protein Solutions ◽  
Solvent Interactions

scholarly journals Thermophoresis: The Case of Streptavidin and Biotin

Polymers ◽  
2020 ◽  
Vol 12 (2) ◽  
pp. 376 ◽  
Author(s):  
Doreen Niether ◽  
Mona Sarter ◽  
Bernd W. Koenig ◽  
Jörg Fitter ◽  
Andreas M. Stadler ◽  
...  
Keyword(s):  
Heavy Water ◽  
Rayleigh Scattering ◽  
Soret Effect ◽  
Binding Constants ◽  
Soret Coefficient ◽  
Protein Solutions ◽  
Elastic Neutron ◽  
Solvent Interactions ◽  
Free Protein ◽  
Promising Tool

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.

Characterization of frozen hydrated biological specimens by low-loss EELS

1992 ◽  
Vol 50 (2) ◽  
pp. 1572-1573
Author(s):  
Songquan Sun ◽  
Richard D. Leapman
Keyword(s):  
Water Content ◽  
Direct Method ◽  
Internal Standard ◽  
Dry Weight ◽  
Dark Field ◽  
Protein Solutions ◽  
Subcellular Compartment ◽  
Differential Shrinkage ◽  
Electron Energy Loss

Analyses of ultrathin cryosections are generally performed after freeze-drying because the presence of water renders the specimens highly susceptible to radiation damage. The water content of a subcellular compartment is an important quantity that must be known, for example, to convert the dry weight concentrations of ions to the physiologically more relevant molar concentrations. Water content can be determined indirectly from dark-field mass measurements provided that there is no differential shrinkage between compartments and that there exists a suitable internal standard. The potential advantage of a more direct method for measuring water has led us to explore the use of electron energy loss spectroscopy (EELS) for characterizing biological specimens in their frozen hydrated state.We have obtained preliminary EELS measurements from pure amorphous ice and from cryosectioned frozen protein solutions. The specimens were cryotransfered into a VG-HB501 field-emission STEM equipped with a 666 Gatan parallel-detection spectrometer and analyzed at approximately −160 C.

Heats of Solution of Some Sodium and Potassium Salts in Water and in Water-Methanol Mixtures

1992 ◽  
Vol 57 (11) ◽  
pp. 2227-2234 ◽  
Author(s):  
Ján Benko ◽  
Oľga Vollárová
Keyword(s):  
Transfer Functions ◽  
Enthalpies Of Solution ◽  
Potassium Salts ◽  
Solvent Interactions ◽  
Heats Of Solution ◽  
Solvent Molecules ◽  
Sodium And Potassium

The enthalpies of solution ∆Hs0 were determined for NaSCN, KSCN, NaBrO3, KBrO3, NaClO3, KClO3, NaIO4, KMnO4, KNO2 and NaNO2 in water-methanol mixtures. The transfer functions ∆Ht0 of the salts and anions were calculated based on the extrathermodynamic TPTB assumption. The ∆Ht0 values of the anion obtained from the sodium and potassium salts were compared. The differences observed, particularly at higher concentrations of the cosolvent, are discussed with respect to the interactions between the solvent molecules and the solute-solvent interactions.

A Comparative Study of Adsorption of Aliphatic Amines at a Gold Electrode

2005 ◽  
Vol 70 (12) ◽  
pp. 2027-2037 ◽  
Author(s):  
Teresa Łuczak
Keyword(s):  
Gibbs Energy ◽  
Comparative Study ◽  
Gold Electrode ◽  
Surface Coverage ◽  
Standard Gibbs Energy ◽  
Gold Surface ◽  
Experimental Dependence ◽  
Aliphatic Amines ◽  
Solvent Interactions ◽  
Amine Concentration

Adsorption of aliphatic amines (C1-C4) at the gold electrode was studied by tensammetry. It has been established that the experimental dependence between the gold surface coverage (Θ) and the bulk amine concentration (cA) fits satisfactorily both by the Frumkin and Flory-Huggins isotherms. The standard Gibbs energy of adsorption, ∆G°ad at Emax for Θ < 0.8 has been found to increase in the order methylamine < ethylamine < propylamine < butylamine. This is rationalised in terms of surface-adsorbate, adsorbate-adsorbate and adsorbate-solvent interactions.

Transfer Thermodynamic Functions ∆Gt0, ∆Ht0 and T∆St0 of cis- and trans-[CoCl2(en)2]+ Isomers in Aqueous Mixtures of Methanol, tert-Butyl Alcohol and Acetonitrile

2000 ◽  
Vol 65 (9) ◽  
pp. 1455-1463
Author(s):  
Oľga Vollárová ◽  
Ján Benko
Keyword(s):  
Enthalpy Of Solution ◽  
Transfer Functions ◽  
Partial Molar Volumes ◽  
Butyl Alcohol ◽  
Aqueous Mixtures ◽  
Aqueous Methanol ◽  
Solvent Interactions ◽  
Tert Butyl Alcohol ◽  
Surface Charge Distribution ◽  
Cis And Trans

The solubility, partial molar volume and standard integral molar enthalpy of solution of cis- and trans-[CoCl2(en)2]Cl in water, aqueous methanol, aqueous tert-butyl alcohol and aqueous acetonitrile are reported. The transfer functions ∆Gt0, ∆Ht0 and T∆St0 as well as partial molar volumes are used to obtain information on the solute-solvent interactions. Results obtained are discussed in terms of differences in the surface charge distribution in isomeric coordination species.

scholarly journals THE REFRACTIVITY OF PROTEIN SOLUTIONS

1935 ◽  
Vol 108 (3) ◽  
pp. 703-707
Author(s):  
David B. Hand
Keyword(s):  
Protein Solutions

scholarly journals The Different Colors of mAbs in Solution

Antibodies ◽  
2021 ◽  
Vol 10 (2) ◽  
pp. 21
Author(s):  
Alexandre Ambrogelly
Keyword(s):  
Visual Inspection ◽  
Quantitative Methods ◽  
Geographical Area ◽  
Therapeutic Protein ◽  
Protein Solutions ◽  
Protein Solution ◽  
Critical Quality Attribute ◽  
Recombinant Therapeutic Protein ◽  
Protein Variants ◽  
Antibody Solution

The color of a therapeutic monoclonal antibody solution is a critical quality attribute. Consistency of color is typically assessed at time of release and during stability studies against preset criteria for late stage clinical and commercial products. A therapeutic protein solution’s color may be determined by visual inspection or by more quantitative methods as per the different geographical area compendia. The nature and intensity of the color of a therapeutic protein solution is typically determined relative to calibrated standards. This review covers the analytical methodologies used for determining the color of a protein solution and presents an overview of protein variants and impurities known to contribute to colored recombinant therapeutic protein solutions.

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