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Luminescence Resonance Energy Transfer to Study Conformational Changes in Membrane Proteins Expressed in Mammalian Cells
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Luminescence Resonance Energy Transfer to Study Conformational Changes in Membrane Proteins Expressed in Mammalian Cells

Article DOI: 10.3791/51895-v • 08:31 min • September 16th, 2014
September 16th, 2014 •
1, 1, 1
1Center for Membrane Biology, Department of Biochemistry and Molecular Biology, University of Texas Health Science Center at Houston

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We describe here an improved Luminescence Resonance Energy Transfer (LRET) method where we introduce a protease cleavage site between the donor and acceptor fluorophore sites. This modification allows us to obtain specific LRET signals arising from membrane proteins of interest, allowing for the study of membrane proteins without protein purification.

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Luminescence Resonance Energy Transfer LRET Conformational Changes Membrane Proteins Mammalian Cells Distance Measurement Ligated Conditions Lanthanide Donor Fluorophore Terbium Chelation Acceptor Fluorophores Sensitized Acceptor Emission Protease Cleavage Site Background Signal Subtraction Physiologically Relevant Measurements
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