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. Author manuscript; available in PMC: 2022 Apr 9.
Published in final edited form as: Methods Enzymol. 2021 Apr 9;654:407–434. doi: 10.1016/bs.mie.2021.03.008

Table 1.

Genetic manipulations for altering BacNav biophysical properties.

Mutation Intended effects
Altering membrane voltage dependencies of BacNav activation and inactivation
D60X Right-shifted inactivation (via substitution by neutral and positive amino acids) (Shimomura et al., 2011)
E43X Right-shifted inactivation (via substitution by neutral and positive amino acids) (Shimomura et al., 2011)
E70X or D91X Left-shifted activation (via substitution by neutral and positive amino acids) (Blanchet et al., 2007)
D237G, E238G, E239G Left-shifted activation (Shaya et al., 2014)
M232A Left-shifted activation (Shaya et al., 2014)
R110C, R113C, R116C, R119C These are gating charges of the voltage-sensing domain. Right-shifted inactivation via substitution by neutral amino acids (Chahine, Pilote, Pouliot, Takami, & Sato, 2004)
Speeding up gating kinetics
L64T Faster activation and inactivation kinetics via substitution by hydrophilic amino acids (Lacroix, Campos, Frezza, & Bezanilla, 2013)
F218A Faster activation and inactivation kinetics
A216G Faster inactivation kinetics (Irie et al., 2010)

Note: The amino acid residues shown in table are based on NavSheP. The actual position may vary in different BacNav orthologs.