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Originally Posted by GAHD Probably just off the wall
I read it earlyer and I've been thinking it over, and so far I'm thinking the answer is a resounding "no" because the proteines would have the carbon locked into their structure; not locked directly to the other carbon atoms as a CNT requires. the whole magic of CNts is that the carbon connect to other carbon and *only* other carbon using up all it's 'free' electrons in the process. In so doing, the carbon creates a strong structure. |
Sorry for the impatience
My rather simplistic view of chemistry should prove rather interesting, if not humorous.
What I had in mind was a protein that would self polymerize helically in the presence of something like a benzene molecule (Likely there are much better choices out there), creating a lining of hydrocarbons on the interior of the helical structure.
A process of depolymerizing should remove the protein as well as the hydrogen atoms, leaving the carbon to bond with the carbon.
Ideally, the bacteria should produce, and expel the protein to the external environment. that way the depolymerizing and cracking process could take advantage of current industrial methods.
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Originally Posted by Racoon
Made to do whuh??
Actin ; as in Actin-Myosin crossbridge, like in human myofibrils?
that protein?
proteins aren't bacteria the last time someone thumped me on the head...
Sounds like you got some cool ideas..., up in B.C.
need more clarification. |
Yes Racoon, that Actin

Proteins are not bacteria, but bacteria can produce proteins. The intent was that the bacteria would be the fabricator for the proteins.