## Abstract Fragments of G protein‐coupled receptors (GPCRs) are widely used as models to investigate these polytopic integral–membrane, signal‐transducing molecules, but have proven difficult to prepare in quantities necessary for NMR analyses. We report on the biosynthesis of two double transmemb
Large multiple transmembrane domain fragments of a G protein-coupled receptor: Biosynthesis, purification, and biophysical studies
✍ Scribed by Zhanna Potetinova; Subramanyam Tantry; Leah S. Cohen; Katrina E. Caroccia; Boris Arshava; Jeffrey M. Becker; Fred Naider
- Book ID
- 115550942
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 2012
- Tongue
- English
- Weight
- 874 KB
- Volume
- 98
- Category
- Article
- ISSN
- 0006-3525
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
## Abstract The α‐factor receptor(Ste2p) is required for the sexual conjugation of the yeast Saccharomyces cerevisiae. Ste2p belongs to the G protein‐coupled receptor (GPCR) family sharing a common heptahelical transmembrane structure. Biological synthesis of regions of Ste2p fused to a leader prot
## Abstract The cannabinoid receptor subtype 2 (CB2) is a member of the G‐protein coupled receptor (GPCR) superfamily. As the relationship between structure and function for this receptor remains poorly understood, the present study was undertaken to characterize the structure of a segment includin
## Abstract Transmembrane domains (TMDs) of G‐protein coupled receptors (GPCRs) have very low water solubility and often aggregate during purification and biophysical investigations. To circumvent this problem many laboratories add oligolysines to the __N__‐ and __C__‐termini of peptides that corre