In particular, we describe how certain energase actions and vibrationally assisted tunneling may influence the conformational dynamics of the neuronal cytoskeletal protein network.
Keywords: soliton, energase, microtubule, SNARE complex.
Formally, the mechanism of the tubulin tail breathing action could be manifestly a form of enzymatic energase process.
Since it had been already observed that in stable microtubules there is no possibility for tubulin bound nucleotide cycling, we propose that tubulin tail energase action releases the energy accumulated in metastable conformational states of kinesin, dynein, or phosphorylated MAPs.
To this extent, in Georgiev (2004, 2003a) several possibilities involving sine-Gordon kinkantikink--breather soliton collisions were proposed, where for instance, a standing breather soliton could be coupled to the energase action of the tubulin tails through vibrationally assisted tunneling.