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ULTIMATE COMPUTING - Quantum Consciousness Studies

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98 Cytoskeleton/Cytocomputer<br />

requires contractile MAPs spaced between 15 and 25 nanometers apart along MT<br />

lengths. Many other MAP binding patterns are spirals which wind around MT<br />

cylinders in super-helices, and several theories suggest how these sites can be<br />

determined. These include linear sequencing of varying tubulin isozymes along<br />

protofilaments (Kim, 1986), crystal symmetry describing each MAP terrain<br />

(Figure 5.17, Koruga, 1986) or by the lattice steps necessary to get from one MAP<br />

site to its nearest neighbor MAP. For example, electron micrographs of MAP-MT<br />

binding by Burns (1978) clearly show MAP binding which may be described as<br />

“over 3, up 1.” That is, if the tubulin subunit to which the MAP is bound is the<br />

starting point, moving 3 monomers along the leftward row helix, and then up 1<br />

monomer along the protofilament will indicate the next attachment site. A number<br />

of geometrical super-helical patterns have been observed which match other<br />

“chess-like” movement rules. These are shown in Figures 5.12–5.15. In other<br />

instances such as brain MAPs, attachment patterns are irregular and<br />

heterogeneous, and thus are capable of representing information.<br />

Figure 5.13: Patterns of MAP attachment to microtubules observed by electron<br />

microscopy (Burns, 1978; Kim et al., 1986; and others).<br />

Rod shaped bridges which occur between MT are of at least two sorts. Motion<br />

producing protein “arms” which consume ATP hydrolysis energy to generate<br />

force are analogous to myosin bridges of skeletal muscle. Moving arms attached<br />

to MT are made of proteins called kinesin and dynein. Dynein arms on MT which<br />

contract in organized sequences to produce collective movements were first<br />

described and characterized in cilia and flagella by Ian Gibbons (1968). The arms<br />

reside at periodic intervals along the outer MT within cilia and flagella. They

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