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Data Brief. 2015 Dec 25;6:433-7. doi: 10.1016/j.dib.2015.12.010. eCollection 2016 Mar.

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

Author information

1
Department of Chemistry, University of Puerto Rico, Río Piedras Campus, San Juan, PR, United States.
2
Department of Pharmaceutical Sciences, School of Pharmacy, Medical Sciences Campus University of Puerto Rico, San Juan, PR, United States.
3
Department of Biology, University of Puerto Rico, Río Piedras Campus, San Juan, PR, United States.
4
Department of Physical Sciences, University of Puerto Rico, Río Piedras Campus, San Juan, PR, United States; Molecular Science Building, University of Puerto Rico, San Juan, PR, United States.
5
Department of Biology, University of Puerto Rico, Río Piedras Campus, San Juan, PR, United States; Molecular Science Building, University of Puerto Rico, San Juan, PR, United States.

Abstract

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.

KEYWORDS:

Detergents; Fluorescence recovery after photobleaching; Lipidic Cubic Phase; Planar lipid bilayer; Two-electrode voltage clamp; nAChR

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