F Paramagnetic Relaxation-Based NMR for Quaternary Structural Restraints of Ion Channels.

Clicks: 376
ID: 51450
2019
Article Quality & Performance Metrics
Overall Quality
Not rated
Combines reader engagement with the AI quality analysis. This article has not been analysed, so there is no overall score — reader engagement is measured and shown alongside.
AI Quality Assessment
Not analyzed
Readership in this journal
Emerging

Ranked #7 of 265 articles by views in ACS chemical biology

Most read Least read

Bar heights use a square-root scale. Only the 120 most-read articles are drawn; the journal has 265 in total.

Mint this article as an NFT
Not yet minted

Create a permanent, verifiable on-chain record of this article on the Scimatic Network. The NFT is held in your Journament account, and you can withdraw it to your own wallet at any time.

5 SUSD one-off · no wallet required
Abstract
Quaternary distance restraints are essential to define the three-dimensional structures of protein assemblies. These distances often fall within a range of 10-18 Å, which challenges the high and low measurement limits of conventional nuclear magnetic resonance (NMR) and double electron-electron resonance electron spin resonance spectroscopies. Here, we report the use of F paramagnetic relaxation enhancement (PRE) NMR in combination with F/paramagnetic labeling to equivalent sites in different subunits of a protein complex in micelles to determine intersubunit distances. The feasibility of this strategy was evaluated on a pentameric ligand-gated ion channel, for which we found excellent agreement of the F PRE NMR results with previous structural information. The study suggests that F PRE NMR is a viable tool in extracting distance restraints to define quaternary structures.
Reference Key
bondarenko2019facs Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Bondarenko, Vasyl;Wells, Marta M;Chen, Qiang;Singewald, Kevin C;Saxena, Sunil;Xu, Yan;Tang, Pei;
Journal ACS chemical biology
Year 2019
DOI
10.1021/acschembio.9b00692
URL
Keywords Keywords not found

Citations

No citations found. To add a citation, contact the admin at info@scimatic.org

No comments yet. Be the first to comment on this article.