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. Author manuscript; available in PMC: 2021 Jul 16.
Published in final edited form as: Biochemistry. 2020 Aug 17;59(33):3051–3059. doi: 10.1021/acs.biochem.0c00526

Figure 1.

Figure 1.

Sequence comparison of VIPER and MiniVIPER. Helical wheel diagrams of (A) VIPER and (B) MiniVIPER were generated using DrawCoil 1.0 (https://grigoryanlab.org/drawcoil/). Charged residues are colored red or blue, with salt bridges indicated by dashed lines. Polar residues are colored orange, and hydrophobic residues are colored gray. Residues altered in MiniVIPER are denoted with an asterisk. (C) Sequences of VIP tags and probes, with coil-forming amino acids in bold. The fifth heptad in CoilE and CoilR, which was removed in MiniE and MiniR, is indicated by a dashed line. Other changes to the MiniVIPER sequences are underlined in green.