Cargando…
Probing Arginine Side-Chains and Their Dynamics with Carbon-Detected NMR Spectroscopy: Application to the 42 kDa Human Histone Deacetylase 8 at High pH**
Autores principales: | Werbeck, Nicolas D, Kirkpatrick, John, Hansen, D Flemming |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
WILEY-VCH Verlag
2013
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4016738/ https://www.ncbi.nlm.nih.gov/pubmed/23401322 http://dx.doi.org/10.1002/anie.201209385 |
Ejemplares similares
-
Loop Interactions
and Dynamics Tune the Enzymatic
Activity of the Human Histone Deacetylase 8
por: Kunze, Micha B. A., et al.
Publicado: (2013) -
Using (15)N-Ammonium to Characterise and Map Potassium Binding Sites in Proteins by NMR Spectroscopy
por: Werbeck, Nicolas D, et al.
Publicado: (2014) -
The 37kDa/67kDa Laminin Receptor acts as a receptor for Aβ(42) internalization
por: Da Costa Dias, Bianca, et al.
Publicado: (2014) -
Structural Analysis of the 42 kDa Parvulin of Trypanosoma brucei
por: Rehic, Edisa, et al.
Publicado: (2019) -
A distal regulatory region of a class I human histone deacetylase
por: Werbeck, Nicolas D., et al.
Publicado: (2020)