Figure 5
From: Comparisons of the M1 genome segments and encoded μ2 proteins of different reovirus isolates
Secondary structure predictions of μ2 protein. (A) Hydropathicity index predictions of T2J (- - -) and T1L (-----) μ2 proteins, superimposed to accentuate similarities and differences. Hydropathy values were determined by the Kyte-Doolittle method [72], using DNA Strider 1.2, a window length of 11, and a stringency of 7. (B) Surface probability predictions of the T2J μ2 protein, determined as per Emini et al. [73], using DNASTAR. The predicted surface probability profiles of T1L and T3D (not shown) were identical to T2J. (C) Locations of α-helices and β-sheets were determined by the PHD PredictProtein algorithms [74], and results were graphically rendered with Microsoft PowerPoint software.
, α-helix;.
, β-sheet;—, turn. Differences in fill pattern correspond to arbitrary division of protein into four regions; N, amino terminal; V, variable; H, helix-rich; C, carboxyl terminal. The locations of variable regions are indicated by the thick lines under the domain representation.