Cargando…
Aromatic ring flips in differently packed ubiquitin protein crystals from MAS NMR and MD
Probing the dynamics of aromatic side chains provides important insights into the behavior of a protein because flips of aromatic rings in a protein’s hydrophobic core report on breathing motion involving a large part of the protein. Inherently invisible to crystallography, aromatic motions have bee...
Autores principales: | Gauto, Diego F., Lebedenko, Olga O., Becker, Lea Marie, Ayala, Isabel, Lichtenecker, Roman, Skrynnikov, Nikolai R., Schanda, Paul |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9791609/ https://www.ncbi.nlm.nih.gov/pubmed/36578472 http://dx.doi.org/10.1016/j.yjsbx.2022.100079 |
Ejemplares similares
-
Assignment of aromatic side-chain spins and characterization of their distance restraints at fast MAS
por: Ahlawat, Sahil, et al.
Publicado: (2022) -
SAA fibrils involved in AA amyloidosis are similar in bulk and by single particle reconstitution: A MAS solid-state NMR study
por: Sundaria, Arpita, et al.
Publicado: (2022) -
In-cell DNP NMR reveals multiple targeting effect of antimicrobial peptide
por: Separovic, Frances, et al.
Publicado: (2022) -
Biological solid-state NMR: Integrative across different scientific disciplines
por: Baldus, Marc
Publicado: (2022) -
Solid-state NMR analysis of unlabeled fungal cell walls from Aspergillus and Candida species
por: Fernando, Liyanage D., et al.
Publicado: (2022)