Cargando…
Fluorine NMR Spectroscopy Enables to Quantify the Affinity Between DNA and Proteins in Cell Lysate
The determination of the binding affinity quantifying the interaction between proteins and nucleic acids is of crucial interest in biological and chemical research. Here, we have made use of site‐specific fluorine labeling of the cold shock protein from Bacillus subtilis, BsCspB, enabling to directl...
Autores principales: | Welte, Hannah, Sinn, Pia, Kovermann, Michael |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8596521/ https://www.ncbi.nlm.nih.gov/pubmed/34390111 http://dx.doi.org/10.1002/cbic.202100304 |
Ejemplares similares
-
Insights into Protein Stability in Cell Lysate by (19)F NMR Spectroscopy
por: Welte, Hannah, et al.
Publicado: (2020) -
What does fluorine do to a protein? Thermodynamic, and highly-resolved structural insights into fluorine-labelled variants of the cold shock protein
por: Welte, Hannah, et al.
Publicado: (2020) -
All atom insights into the impact of crowded environments on protein stability by NMR spectroscopy
por: Köhn, Birgit, et al.
Publicado: (2020) -
Synthesis of fluorinated maltose derivatives for monitoring protein interaction by (19)F NMR
por: Braitsch, Michaela, et al.
Publicado: (2012) -
Fluoroacetamide Moieties as NMR Spectroscopy Probes for the Molecular Recognition of GlcNAc‐Containing Sugars: Modulation of the CH–π Stacking Interactions by Different Fluorination Patterns
por: Unione, Luca, et al.
Publicado: (2017)