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. Author manuscript; available in PMC: 2008 Sep 1.
Published in final edited form as: Biochim Biophys Acta. 2007 Jun 29;1774(9):1213–1220. doi: 10.1016/j.bbapap.2007.06.002

Fig. 1.

Fig. 1

Multiple sequence alignment of human R4-subfamily RGS proteins RGS4, −8, −16, and the RZ-subfamily member RGS19. (A) Solvent-accessible residues within RGS4 are demarcated by “o” (outside), while internal residues are noted by “i” (inside) and partially solvent-exposed residues are unlabeled, as predicted by the GETAREA 1.1 algorithm [20] using a solvent probe of 1.40 Å as applied to the high-resolution structure of free RGS4 [21]. Position of Cys-71 and Cys-132, found uniquely within RGS4, are indicated by arrowheads. Alpha-helices observed within the NMR structures of RGS4 and RGS19 [21, 25] are numbered in Roman numerals. (B) Equivalent purification of wildtype and cysteine point-mutant RGS4 and RGS8 proteins for biochemical and mass spectrometry analyses is highlighted by coomassie blue staining of SDS-PAGE resolved proteins.