Cargando…
Thermophoresis: The Case of Streptavidin and Biotin
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 se...
Autores principales: | Niether, Doreen, Sarter, Mona, Koenig, Bernd W., Fitter, Jörg, Stadler, Andreas M., Wiegand, Simone |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7077373/ https://www.ncbi.nlm.nih.gov/pubmed/32046223 http://dx.doi.org/10.3390/polym12020376 |
Ejemplares similares
-
Cooperative Change
in the Internal Dynamics of Streptavidin
Caused by Biotin Binding
por: Sarter, Mona
Publicado: (2023) -
A biotin-streptavidin-biotin bridge dramatically enhances cell fusion
por: LI, JINHUA, et al.
Publicado: (2014) -
Development and Evaluation of an Anti-Biotin Interference Method in Biotin-Streptavidin Immunoassays
por: Liu, Dong, et al.
Publicado: (2022) -
Functional Loop Dynamics of the Streptavidin-Biotin Complex
por: Song, Jianing, et al.
Publicado: (2015) -
Chemistry of Biotin–Streptavidin
and the Growing
Concern of an Emerging Biotin Interference in Clinical Immunoassays
por: Luong, John H. T., et al.
Publicado: (2019)