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Expression and Purification of CB2 for NMR Studies in Micellar Solution

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Abstract:

We demonstrate feasibility of biophysical characterization of the peripheral cannabinoid receptor CB2 produced by heterologous expression in E. coli membranes. Recombinant receptor was purified by affinity chromatography, and NMR diffusion experiments performed on CB2 solubilized in dodecylphosphocholine (DPC) micelles. Circular dichroism spectroscopy indicated high α-helical content (49 %) of CB2.





Keywords: 1H NMR; Cannabinoid receptor CB2; circular dichroism spectroscopy; dodecylphosphocholine micelles; ligand binding

Document Type: Research Article

DOI: https://doi.org/10.2174/092986607782541051

Publication date: 2007-10-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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