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- Hernaiz, M., et al.
(författare)
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The contact angle of nanofluids as thermophysical property
- 2019
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Ingår i: Journal of Colloid and Interface Science. - : Elsevier BV. - 0021-9797. ; 547, s. 393-406
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Tidskriftsartikel (refereegranskat)abstract
- Droplet volume and temperature affect contact angle significantly. Phase change heat transfer processes of nanofluids – suspensions containing nanometre-sized particles – can only be modelled properly by understanding these effects. The approach proposed here considers the limiting contact angle of a droplet asymptotically approaching zero-volume as a thermophysical property to characterise nanofluids positioned on a certain substrate under a certain atmosphere. Graphene oxide, alumina, and gold nanoparticles are suspended in deionised water. Within the framework of a round robin test carried out by nine independent European institutes the contact angle of these suspensions on a stainless steel solid substrate is measured with high accuracy. No dependence of nanofluids contact angle of sessile droplets on the measurement device is found. However, the measurements reveal clear differences of the contact angle of nanofluids compared to the pure base fluid. Physically founded correlations of the contact angle in dependency of droplet temperature and volume are obtained from the data. Extrapolating these functions to zero droplet volume delivers the searched limiting contact angle depending only on the temperature. It is for the first time, that this specific parameter, is understood as a characteristic material property of nanofluid droplets placed on a certain substrate under a certain atmosphere. Together with the surface tension it provides the foundation of proper modelling phase change heat transfer processes of nanofluids.
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| 2. |
- Rich, Rebecca L., et al.
(författare)
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A global benchmark study using affinity-based biosensors
- 2009
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Ingår i: Analytical Biochemistry. - : Elsevier BV. - 0003-2697 .- 1096-0309. ; 386:2, s. 194-216
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Tidskriftsartikel (refereegranskat)abstract
- To explore the variability in biosensor studies, 150 participants from 20 countries were given the same protein samples and asked to determine kinetic rate constants for the interaction. We chose a protein system that was amenable to analysis using different biosensor platforms as well as by users of different expertise levels. The two proteins (a 50-kDa Fab and a 60-kDa glutathione S-transferase [GST] antigen) form a relatively high-affinity complex, so participants needed to optimize several experimental parameters, including ligand immobilization and regeneration conditions as well as analyte concentrations and injection/dissociation times. Although most participants collected binding responses that could be fit to yield kinetic parameters, the quality of a few data sets could have been improved by optimizing the assay design. Once these outliers were removed, the average reported affinity across the remaining panel of participants was 620 pM with a standard deviation of 980 pM. These results demonstrate that when this biosensor assay was designed and executed appropriately, the reported rate constants were consistent, and independent of which protein was immobilized and which biosensor was used.
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