ISIS Neutron and Muon Source Data Journal

Adsorption of NHE1 intracellular domain on lipid bilayers

Abstract: Recently the intracellular domain (ICD ) of the Na+/H+ exchanger isoform 1 (NHE1), is a transmembrane protein, has been identified as an intrinsically disordered protein. NHE1/ICD regulates protein activity via binding of other proteins, kinases or calmodulin, as well as by interacting with the anionic phospholipids in the membrane. Although a specific lipid interaction domain (LID) in NHE1/ICD (named here after NHE1/LID) was identified, a detailed picture of the mechanism of interaction between the lipids in the membrane and NHE1/LID is still missing. We propose to collect structural data on NHE1/LID interaction with supported lipid bilayer (POPC and POPC/POPS) by means of Neutron Reflectometry. This data will complement our previous results and are aimed at characterizing the protein adsorption processes as well as at locating the adsorbed protein with respect to the membrane.

Principal Investigator: Dr Alessandra Luchini
Local Contact: Dr Arwel Hughes
Experimenter: Professor Lise Arleth
Experimenter: Dr Raul Araya Secchi
Experimenter: Mr Frederik Tidemand
Experimenter: Mr Nicolai Johansen

DOI: 10.5286/ISIS.E.RB1810880

ISIS Experiment Number: RB1810880

Publisher: STFC ISIS Neutron and Muon Source

Data format: RAW/Nexus
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Data Citation

The recommended format for citing this dataset in a research publication is as:
[author], [date], [title], [publisher], [doi]

For Example:
Dr Alessandra Luchini et al; (2018): Adsorption of NHE1 intracellular domain on lipid bilayers, STFC ISIS Neutron and Muon Source, https://doi.org/10.5286/ISIS.E.RB1810880

Data is released under the CC-BY-4.0 license.