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. Author manuscript; available in PMC: 2013 Aug 1.
Published in final edited form as: Protein Expr Purif. 2012 Jun 19;84(2):224–235. doi: 10.1016/j.pep.2012.06.005

Fig. 5.

Fig. 5

Circular dichroism spectroscopy of A2aR TM 7 indicates α-helical secondary structure. SDS–PAGE (16% acrylamide) shows that purified and dialyzed hA2aR TM 7 peptide forms dimers through a disulfide bond, where addition of DTT reduces these intermolecular bonds (A). Purified hA2aR TM 7 was diluted to 41.4 μM in 20mM phosphate buffer, pH 7.4, 0.1% Fos-choline 16 with (closed circles) and without (open circles) 5 mM TCEP and characterized by CD (B). Fusion protein (FP); monomeric hA2aR TM 7 peptide (P-M); putative dimeric hA2aR TM 7 peptide (P-D) are indicated with arrows.