TUBULIN PROTEIN AND INFORMATION PROCESSING

Biological conscious behavior is associated with human brain activity and inactivity which can be understood by conscious mind studies. Human brain and conscious mind studies have a correlation with microtubules, therefore, these studies are done on the basis of microtubules alignment, their association with other proteins and formulation. Protein conformation dynamics (regulated by quantum mechanical van der Waals London forces) are responsible for the activities in living cells. Quantum Hopfield network model of the brain explains five levels of neural interaction for learning and association [1]. Microtubules having diameter of 25 nanometers comprises to be the largest cytoskeleton filament. Alpha and beta tubulin are the two subunits of microtubules, forms a heterodimer. The present work focuses on the topology of Microtubule Associated Proteins (MAPs) and tubulin protein. The study also includes the understanding of interaction of tubulin with MAP-tau and Anti-Tau with the help of I-Tasser and PyMOL methods separately. Models of MAPs with C-Score < -1.5 is considered to be the most acceptable model. PyMol study helped in constructing a 3D structure of tubulin protein and its interaction with Tau and Anti-Tau and thereby, helped in visualizing the binding site or preference of interaction at specific position of protein. Memory, learning and information processing are interrelated and microtubules/tubulin plays a key role in all these processes. Tau aggregation is linked to neurodegeneration and clinical manifestations of Alzheimer's Disease, a memory loss disease. PyMOL study showed strong interaction of tubulin with Anti-Tau, an antibody. This antibody against tau can prevent the trans-synaptic transmission of tau between neurons and hence memory (information processing) can be regained.