Transporter stability

Several /i-solenoid domains appear to promote the oligomerization of multidomain proteins. There are at least three types of /i-solenoid association. First, oligomers (dimers or trimers) are formed by lateral interaction of the solenoids. For example, the C-terminal domain of the bacterial cell division inhibitor MinC is a short right-handed T-type solenoid with an apolar lateral face that mediates homodimerization (Cordell et al., 2001). Trimers of several bacterial transferases are formed by lateral, in-register, interaction of left-handed T-type /1-solenoids (Fig. 5). Second, dimers may form via interactions of the open terminal coils of /1-solenoids as in the dimeric structure of iron transporter stabilizer SufD (Badger et al., 2005). Finally, dimerization may be mediated by swapping of /1-strands of the terminal coils, as in the CAP (Dodatko et al., 2004) (Fig. S). 

Effective properties (proton and water transport, stability)... 

Ion Transport Stability Adhesion Multienzyme and Multilayer Configurations Immobilization of Redox Mediators Derivatization of Monomers before Conducting Polymer Electrosynthesis Direct Electrical Modulation of Enzymes Electroactive Polymer Hydrogels... 

Usually, an addition of semiconductor NCs into conducting polymer ensures improvement of charge transport, stability characteristics, and EL efficiency of these devices as compared to pure conducting polymer. 

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