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Fig. 3 | BMC Structural Biology

Fig. 3

From: Classification of the human THAP protein family identifies an evolutionarily conserved coiled coil region

Fig. 3

Prediction of secondary structure of THAP proteins. Predicted alpha helical regions are (a) sTHAP protein group: residues 143–188 (THAP1), 135–178 (THAP2), 189–224 (THAP3) and 148–193 (THAP6) (b) mTHAP protein group: residues 237–281 (THAP7), 180–209 (THAP8) and 254–310 (THAP11) (c) lTHAP protein group: residues 150–180 (THAP0), 362–398 (THAP4), 331–372 (THAP5) and 145–182 (THAP9). The secondary structure predicted by JPRED assigns a score from 0 to 9 for a predicted helix forming region, 0 being the lowest and 9 being the highest probability of forming a helix. The Heptad pattern is as described in Additional file 1: Figure S1a

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