Thermophoresis: The Case of Streptavidin and Biotin.
hydrogen bonds
protein–ligand binding
thermophoresis
Journal
Polymers
ISSN: 2073-4360
Titre abrégé: Polymers (Basel)
Pays: Switzerland
ID NLM: 101545357
Informations de publication
Date de publication:
07 Feb 2020
07 Feb 2020
Historique:
received:
11
12
2019
revised:
27
01
2020
accepted:
29
01
2020
entrez:
13
2
2020
pubmed:
13
2
2020
medline:
13
2
2020
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 32046223
pii: polym12020376
doi: 10.3390/polym12020376
pmc: PMC7077373
pii:
doi:
Types de publication
Journal Article
Langues
eng
Subventions
Organisme : Bundesministerium für Bildung und Forschung
ID : 05K16PA1
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