Functionality and stability data of detergent purified nAChR from Torpedo using lipidic matrixes and macroscopic electrophysiology | Zendy

Luis F. Padilla-Morales | Zendy; José O. ColónSáez | Zendy; Joel E. González-Nieves | Zendy; Orestes Quesada-González | Zendy; José A. LasaldeDominicci | Zendy

Open Access

Functionality and stability data of detergent purified nAChR from Torpedo using lipidic matrixes and macroscopic electrophysiology

Author(s) -

Luis F. Padilla-Morales,

José O. ColónSáez,

Joel E. González-Nieves,

Orestes Quesada-González,

José A. LasaldeDominicci

Publication year - 2015

Publication title -

data in brief

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.122

H-Index - 30

ISSN - 2352-3409

DOI - 10.1016/j.dib.2015.12.010

Subject(s) - torpedo , acetylcholine receptor , voltage clamp , chemistry , membrane , nicotinic acetylcholine receptor , fluorescence recovery after photobleaching , chromatography , lipid bilayer , biophysics , photobleaching , electrophysiology , membrane potential , biochemistry , receptor , biology , fluorescence , physics , quantum mechanics , neuroscience

The presented data provides additional information about the assessment of affinity purified nicotinic acetylcholine receptor (nAChR) rich membrane solubilized with long chain (16 saturated carbons) lysophospholipid with glycerol headgroup (LFG-16). The assessment of stability and functionality of solubilized membrane protein is a critical step prior to further crystallization trails. One of the key factors for this task is the appropriate choice of a detergent that can support nAChR activity and stability comparable to the crude membranes. The stability of the nAChR-LFG-16 complex incorporated into lipid cubic phase (LCP) was monitored for a period of 30 days by means of fluorescence recovery after photobleaching (FRAP) and the functionality was evaluated after its incorporation into Xenopus oocyte by means of the two electrode voltage clamp technique.

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