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- From: ian@inf.ethz.ch (Ian)
- Newsgroups: sci.nanotech
- Subject: Re: Organic Machines?
- Message-ID: <Jan.25.17.25.47.1993.10293@planchet.rutgers.edu>
- Date: 25 Jan 93 22:25:48 GMT
- Sender: nanotech@planchet.rutgers.edu
- Organization: Dept Biochemistry, University of Bristol, UK
- Lines: 71
- Approved: nanotech@aramis.rutgers.edu
-
- In article <Jan.21.23.07.19.1993.5333@planchet.rutgers.edu> szabo@techbook.com (Nick Szabo) writes:
- >
- >The second is biotechnology,
- >with liposomes (drug-carrying artificial membranes), monoclonal
- >antibodies (cells programmed to be triggered by specific molecules),
- >polymerase chain reaction (self-replication of DNA outside the cell,
- >greatly accelerated over what nature can do), and gene-splicing
- >as the basis for two new fields, protein engineering and metabolic
- >engineering.
-
- What do you refer to as 'metabolic engineering' ? It's a new phrase to me.
-
- >We can already see these two fields starting to merge. Lithography
- >is being used to program arrays of chemical reactions, for use
- >in DNA sequencing, designer polymers, etc. Enzymes (protein
- >catalysts) have been built into clay structures; these molecular
- >cyborgs now help make such ubiquitious products as the corn syrup in
- >your Pepsi. Soon we will see enzymes designed on a computer,
-
- I don't think that protein-design will become that advanced so soon.
- The problem is terribly difficult, involving:
-
- 1) Analysis of biological catalysis (there are still only a few rigorously
- studied enzymes) and its extension to the design of general new catalysts.
-
- 2) Solving the problem of protein folding/protein local-conformation to the
- point of being able to insert the desired arrangement of catalytic groups
- into a protein framework.
-
- >programmed into DNA by wet-array-lithography,
-
- Why not just use a gene-synthesizer, like we usually do ?
-
- >mass produced by
- >gene-spliced bacteria, and then hooked onto lithographed structures
- >to form catalysts orders of magnitude more proficient than today's.
-
- It depends what you mean by 'proficient' ? Existing enzymes are very
- good catalysts but constrained by the fact that they were produced to meet
- several other requirements besides their basic catalytic role. For example,
- they must be soluble, stable and must'nt bind irrevocably to other cell
- components. Also they must be specific to the desired reaction and must
- ignore other, very similar compounds. Some of they also incorporate
- control mechanisms.
-
- If we were to arrange things so that many of these additional requirements
- were no longer necessary, then we probably could produce superior (=faster)
- catalysts. The question is: would we want to ?
-
- For example, specificity might be a very useful characteristic in an
- industrial situation, why purify the output from one process when the next
- could be made to ignore the impurities ?
-
- I suspect that evolved enzymes (whilst not definitively 'best', that would be
- an unreasonable expectation) are extremely good examples of the art of
- catalysis and that we would be extremely hard-pushed to make more than
- rudimentary improvements.
-
-
-
-
- I guess my real reason for replying to this article was to say that the Nick
- gave an impression of Biotechnology that was very close to being a general
- technique for the design and construction of catalysts. In fact, we are
- still fumbling around at the edges.
-
- I don't want to belittle biotech, however, the compounds that can be
- specifically synthesized by biological methods are two orders of magnitude
- more complex than those that can be made by chemical approaches (ie proteins
- of mol.wt. 30,000 with every atom in the right place). I just didn't want
- anybody to expect too much too soon.
-