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. 2012 Sep;12(5):492–499. doi: 10.1016/j.mito.2012.06.010

Fig. 4.

Fig. 4

Homology modeling of D-MTERF5. (A) Overall structure of D-MTERF5 (residues 62–443 of the mature protein) obtained by comparison with human mTERF, by using the Swiss-Model Automated Protein Modeling Server, in which predicted alpha-helices are in red and beta-sheets are in yellow. (B) Molecular surface of D-MTERF5 colored according to the electrostatic surface potential (blue + 12 kT, red − 12 kT).