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== Secondary Structure and the Thioredoxin Like Fold ==

GPx-1 consists of nine β-strand nine α-helices with four of the helices being of the 310 form (Figure 2). Interestingly two of the β-strands form a parallel β-sheet (Figure 3)[[Image:Beta_sheets3.jpg|300px|~~left~~|thumb|]]. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides (6).

GPx-1 consists of nine β-strand nine α-helices with four of the helices being of the 310 form (Figure 2). Interestingly two of the β-strands form a parallel β-sheet (Figure 3)[[Image:Beta_sheets3.jpg|300px|right|thumb|]]. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (5). However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6). This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (6). A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides (6).

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 == Secondary Structure and the Thioredoxin Like Fold ==
-GPx-1 consists of nine β-strand  nine α-helices with four of the helices being of the 310 form (Figure 2).  Interestingly two of the β-strands form a parallel β-sheet (Figure 3)[[Image:Beta_sheets3.jpg|300px|left|thumb|]]. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (5).  However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6).  This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (6).  A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides (6).
+GPx-1 consists of nine β-strand  nine α-helices with four of the helices being of the 310 form (Figure 2).  Interestingly two of the β-strands form a parallel β-sheet (Figure 3)[[Image:Beta_sheets3.jpg|300px|right|thumb|]]. The classic thioredoxin fold consists of a four stranded β-sheet that is surrounded by three α-helices (5).  However the thioredoxin fold is commonly subject to the insertion of additional secondary structural elements between the second β-strand and the second α-helices (6).  This is seen in GPx-1 as there is an addition of an α-helix and a β-strand between the second β-strand and the second α-helices (6).  A similar insertion is found in peroxiredoxins, a different family of proteins which also catalyze the reduction of hydroperoxides (6).
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