Quick web searches on the topic ribosome all show the same:
the amino acid-loaded tRNA arrives at the ribosome with its
anti-codon first. I think this could be an oversimplification, which
doesn`t take notice to the probable, intuitive fact that the gene is
a blueprint for the protein, a mirror-copy made through evolution.
Say the proteins initially instructed the genes and not vice versa.
Say the food came first, and then the means to carry it.
For such a complex process as translation to proceed without many errors,
there has to be another, more primary mechanism of proofreading. Maybe there is a
closer link between amino acids and the mRNA than previously thought.
My point is that it should be possible to make any short gene sequence
that could match any protein, almost as an antibody. The oligonucleotides
It should be possible to target any protein-markers in any disease,
and hence destroy the culprits. Say, put a virus in a PCR machine and make
cheap copies of tailored antibodies! Or use the new oligo synthesis factories!
I try to explain my theory in this video:
I found these articles supporting my theory about amino acids` binding to their cognate codons:
Reinhold Zieglers veg 14 B
mobile: +47 95 177 433
born: February 7th 1971
A drop of ordinary water-smear on a microscopy slide reveals a pattern:
the bacteria in the water lines up, symbolized like this: o…..o..o…o…o
These lines are best seen at 400x magnification. See example picture at bottom of this page.
My theory / idea is that DNA from ruptured bacteria binds and absorbs proteins
from its own species.
So what? If so, if a nucleic acid can bind to a protein in a coded manner,
then the aptamer technology is the tech of the future.
Say for instance the codon GUG, which codes for the amino acid valine, weakly
binds this amino acid. Symbolized like this: E-<
The codon-amino acid binding gives several combinatorial possibilities with
regard to polar interactions, mechanic fit and R-group placement.
If we can make aptamers tailored to bind specific proteins, then we can
take down any pathogen.
can be found at GenBank: http://www.ncbi.nlm.nih.gov/protein/7769644?ordinalpos=1&itool=EntrezSystem2.PEntrez.Sequence.Sequence_ResultsPanel.Sequence_RVDocSum
My plan is to try to make an array of different aptamers to hit this protein.
The approach I will use is basically to design aptamers that are based on
the amino acids` corresponding codons. In the DNA-aptamers, I will replace
U with T, and in the third wobble-position I will choose the assumed least
interfering base (e.g. T, i.e. Thymine). RNA aptamers can also be used.
There is a chance that the aptamers will match directly.
The matches have to be at accessible parts of the protein`s surface.
The aptamers will be ordered (outsourced), for instance from: http://www.biomers.net/upload/Image/Preislisten/DNA_En_EUR.pdf
or from Eurogentec in San Diego, California:
i.e. monoclonal antibodies.
The stock of different aptamers will be annotated at my portable computer.
Then, step 2, we have to beg institutions which store HIV viruses to test the aptamers in vitro.
The results can be viewed with electron microscopes.
e.g. the 17 aa-sequence in the CD44 protein which is over-expressed on membranes on glioma cancer brain cells.)
This project needs help from media. The headlines could be:
“Burn off money to test HIV drug”
“Find needle in haystack”
Press: “Will this be tested in humans? Will there be marketing? Sales?
Answer: “We will find a balanced solution, it`s fair that developed
countries pay for some of the venture.”
The task will require all communication skills and business intelligence.
It is a bit like cloud computing: once the hidden codes are found,
they have to be administered.
It is my goal to reach this goal of my life!
or GGU UGG UGU GGU UGG (in RNA) corresponds to the amino acids:
gly trp cys gly trp abbreviations:
G W C G W
This aptamer bind to the blood coagulation factor protein thrombin.
I found it at:
To find the amino acid sequence in thrombin, I search GenBank at:
The combination “GW” occurred once in the thrombin protein,
the combination “WG” occurred twice,
the combination “WC” occurred twice,
the combination “GC” occurred twice,
and the combination “CG” occurred three times.
I did not find similar matches in the comparable plasma proteins albumin or insulin,
and I think further research will find no other similar matches either.
For pictures of bacteria in water, see this site: http://iceberg.dri.edu/blogs4.php
(Regarding autoimmune MS and diabetes:
My idea is to take down the protein markers
which the T-cells home in on when they perform autoimmunity, and/or target the receptors /
surface proteins on the T-cells which they use in this task. At GenBank we can find some of
the needed gene/protein sequences.)
I try to explain my theory in this video: