ArticlePolymers2020
Thermophoresis: The Case of Streptavidin and Biotin.
Article in Polymers, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed.
- Hydrophilicity controls thermodiffusion in alkylammonium chlorides.The European physical journal. E, Soft matter · 2026Article
- Influence of α-Helical Content on the Thermodiffusion of Apomyoglobin.Langmuir : the ACS journal of surfaces and colloids · 2025Article
- Multiphoton lithography with protein photoresists.Materials today. Bio · 2024Article
- Transdermal Drug Delivery Systems: A Focused Review of the Physical Methods of Permeation Enhancement.Advanced pharmaceutical bulletin · 2024Review
- Cooperative Change in the Internal Dynamics of Streptavidin Caused by Biotin Binding.The journal of physical chemistry. B · 2023Article
- Enhanced Enzymatically Amplified Metallization on Nanostructured Surfaces for Multiplexed Point-of-Care Electrical Detection of COVID-19 Biomarkers.Small (Weinheim an der Bergstrasse, Germany) · 2022Article
- Complementary Experimental Methods to Obtain Thermodynamic Parameters of Protein Ligand Systems.International journal of molecular sciences · 2022Article
- Numerical Analysis of Thermophoresis of a Charged Spheroidal Colloid in Aqueous Media.Micromachines · 2021Article
- Thermophoretic Micron-Scale Devices: Practical Approach and Review.Entropy (Basel, Switzerland) · 2020Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
Abstract
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.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.