View Single Post
  #1  
Unread 04-07-2019, 05:52 PM
nmrlearner's Avatar
nmrlearner nmrlearner is offline
Senior Member
 
Join Date: Jan 2005
Posts: 19,913
Points: 193,617, Level: 100
Points: 193,617, Level: 100 Points: 193,617, Level: 100 Points: 193,617, Level: 100
Level up: 0%, 0 Points needed
Level up: 0% Level up: 0% Level up: 0%
Activity: 50.7%
Activity: 50.7% Activity: 50.7% Activity: 50.7%
Last Achievements
Award-Showcase
NMR Credits: 0
NMR Points: 0
Downloads: 0
Uploads: 0
Default Trimethylsilyl reporter groups for NMR studies of conformational changes in G protein-coupled receptors.

Trimethylsilyl reporter groups for NMR studies of conformational changes in G protein-coupled receptors.

Related Articles Trimethylsilyl reporter groups for NMR studies of conformational changes in G protein-coupled receptors.

FEBS Lett. 2019 Apr 05;:

Authors: Hu W, Wang H, Hou Y, Hao Y, Liu D

Abstract
Large membrane proteins such as G Protein-Coupled Receptors (GPCRs) are difficult for NMR study due to severe signal overlaps and unfavorable relaxation properties. We used a trimethylsilyl (TMS) group as a reporter group for 1 H NMR study of conformational changes in proteins, utilizing high-intensity 1 H NMR signals near 0 ppm. The ?2 -Adrenergic Receptor (?2 AR) was labeled with TMS groups at two cysteines located at the cytoplasmic ends of helices VI and VII. Binding of various ligands led to changes in 1 H NMR signals, which manifested that helix VI is sensitive to G protein-specific activation, whereas helix VII is sensitive to ?-arrestin-specific activation. Thus, the TMS group is a useful reporter group in NMR for studying conformational changes in membrane proteins such as GPCRs. This article is protected by copyright. All rights reserved.


PMID: 30953343 [PubMed - as supplied by publisher]



More...
Reply With Quote


Did you find this post helpful? Yes | No