Cargando…
(113)Cd NMR Experiments Reveal an Unusual Metal Cluster in the Solution Structure of the Yeast Splicing Protein Bud31p
Establishing the binding topology of structural zinc ions in proteins is an essential part of their structure determination by NMR spectroscopy. Using (113)Cd NMR experiments with (113)Cd‐substituted samples is a useful approach but has previously been limited mainly to very small protein domains. H...
Autores principales: | van Roon, Anne‐Marie M., Yang, Ji‐Chun, Mathieu, Daniel, Bermel, Wolfgang, Nagai, Kiyoshi, Neuhaus, David |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
WILEY‐VCH Verlag
2015
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4954022/ https://www.ncbi.nlm.nih.gov/pubmed/27478262 http://dx.doi.org/10.1002/ange.201412210 |
Ejemplares similares
-
(113)Cd NMR Experiments Reveal an Unusual Metal Cluster in the Solution Structure of the Yeast Splicing Protein Bud31p**
por: van Roon, Anne-Marie M, et al.
Publicado: (2015) -
Intermolecular Interactions and Protein Dynamics by Solid‐State NMR Spectroscopy
por: Lamley, Jonathan M., et al.
Publicado: (2015) -
Probing Local Backbone Geometries in Intrinsically Disordered Proteins by Cross-Correlated NMR Relaxation**
por: Stanek, Jan, et al.
Publicado: (2013) -
A Molecular Nanotube with Three‐Dimensional π‐Conjugation
por: Neuhaus, Patrik, et al.
Publicado: (2015) -
Spectroscopic and Crystal Field Consequences of Fluoride Binding by [Yb⋅DTMA](3+) in Aqueous Solution
por: Blackburn, Octavia A., et al.
Publicado: (2015)