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Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3
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Documents
- Wood BiomolNMRAss2012
Final published version, 458 KB, PDF document
DOI
- https://doi.org/10.1007/s12104-011-9315-4
Final published version
- Kathleen Wood ,
- Aviv Paz ,
- Klaas Dijkstra ,
- Ruud M Scheek ,
- Renee Otten ,
- Israel Silman ,
- Joel L Sussman ,
- Frans A.A. Mulder
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 (1)H, (13)C and (15)N resonance assignments for the cytoplasmic domain of human neuroligin 3.
| Original language | English |
|---|---|
| Journal | Biomolecular N M R Assignments |
| Volume | 6 |
| Issue | 1 |
| Pages (from-to) | 15-8 |
| Number of pages | 4 |
| ISSN | 1874-2718 |
| DOIs | |
| Publication status | Published - 2012 |
- Amino Acid Sequence, Cell Adhesion Molecules, Neuronal, Cytoplasm, Humans, Membrane Proteins, Molecular Sequence Data, Nerve Tissue Proteins, Nuclear Magnetic Resonance, Biomolecular, Protein Structure, Tertiary
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