Cargando…
Unexpected dynamics in femtomolar complexes of binding proteins with peptides
Ultra-tight binding is usually observed for proteins associating with rigidified molecules. Previously, we demonstrated that femtomolar binders derived from the Armadillo repeat proteins (ArmRPs) can be designed to interact very tightly with fully flexible peptides. Here we show for ArmRPs with four...
Autores principales: | Cucuzza, Stefano, Sitnik, Malgorzata, Jurt, Simon, Michel, Erich, Dai, Wenzhao, Müntener, Thomas, Ernst, Patrick, Häussinger, Daniel, Plückthun, Andreas, Zerbe, Oliver |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2023
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10684580/ https://www.ncbi.nlm.nih.gov/pubmed/38016954 http://dx.doi.org/10.1038/s41467-023-43596-2 |
Ejemplares similares
-
An automated iterative approach for protein structure refinement using pseudocontact shifts
por: Cucuzza, Stefano, et al.
Publicado: (2021) -
Investigation of Elemental Mass Spectrometry in Pharmacology for Peptide Quantitation at Femtomolar Levels
por: Cordeau, Emmanuelle, et al.
Publicado: (2016) -
Side‐chain dynamics of the α(1B)‐adrenergic receptor determined by NMR via methyl relaxation
por: Baumann, Christian, et al.
Publicado: (2023) -
Probing Metal Ion Discrimination in a Protein Designed to Bind Uranyl Cation With Femtomolar Affinity
por: Hoarau, Marie, et al.
Publicado: (2019) -
Femtomolar detection of SARS-CoV-2 via peptide beacons integrated on a miniaturized TIRF microscope
por: Tripathy, Soumya P., et al.
Publicado: (2022)