Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 14-Day Trial for You or Your Team.

Learn More →

Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3

Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of... Neuroligins act as heterophilic adhesion molecules at neuronal synapses. Their cytoplasmic domains interact with synaptic scaffolding proteins, and have been shown to be intrinsically disordered. Here we report the backbone and side chain 1H, 13C and 15N resonance assignments for the cytoplasmic domain of human neuroligin 3. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biomolecular NMR Assignments Springer Journals

Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3

Loading next page...
 
/lp/springer-journals/backbone-and-side-chain-nmr-assignments-for-the-intrinsically-tR6CC3Q7if

References (24)

Publisher
Springer Journals
Copyright
Copyright © 2011 by The Author(s)
Subject
Physics; Polymer Sciences; Biochemistry, general; Biophysics and Biological Physics
ISSN
1874-2718
eISSN
1874-270X
DOI
10.1007/s12104-011-9315-4
pmid
21647611
Publisher site
See Article on Publisher Site

Abstract

Neuroligins act as heterophilic adhesion molecules at neuronal synapses. Their cytoplasmic domains interact with synaptic scaffolding proteins, and have been shown to be intrinsically disordered. Here we report the backbone and side chain 1H, 13C and 15N resonance assignments for the cytoplasmic domain of human neuroligin 3.

Journal

Biomolecular NMR AssignmentsSpringer Journals

Published: Jun 7, 2011

There are no references for this article.