Solid-state NMR spectroscopy based atomistic view of a membrane protein unfolding pathway
Studying the unfolding of membrane proteins in a native-like lipid environment is challenging. Here the authors describe a method combining hydrogen-deuterium exchange and solid-state NMR measurements that allows the characterization of unfolding events in lipid-embedded membrane proteins and use th...
Enregistré dans:
| Auteurs principaux: | Peng Xiao, David Bolton, Rachel A. Munro, Leonid S. Brown, Vladimir Ladizhansky |
|---|---|
| Format: | article |
| Langue: | EN |
| Publié: |
Nature Portfolio
2019
|
| Sujets: | |
| Accès en ligne: | https://doaj.org/article/598def11c2fc4bcd97e663bc018acd2a |
| Tags: |
Ajouter un tag
Pas de tags, Soyez le premier à ajouter un tag!
|
Documents similaires
-
Distinguishing faceted oxide nanocrystals with 17O solid-state NMR spectroscopy
par: Yuhong Li, et autres
Publié: (2017) -
Polar surface structure of oxide nanocrystals revealed with solid-state NMR spectroscopy
par: Junchao Chen, et autres
Publié: (2019) -
The anatomy of unfolding of Yfh1 is revealed by site-specific fold stability analysis measured by 2D NMR spectroscopy
par: Rita Puglisi, et autres
Publié: (2021) -
High-resolution 3D structure determination of kaliotoxin by solid-state NMR spectroscopy.
par: Jegannath Korukottu, et autres
Publié: (2008) -
Rapid and accurate determination of atomistic RNA dynamic ensemble models using NMR and structure prediction
par: Honglue Shi, et autres
Publié: (2020)