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I take protein and amino acid supplements, but I honestly don't know if they do anything.
I have an amino acid missing that you can only get from certain kinds of eggs. So, I've been eating a few eggs.
The study of the amino acid sequence around the disulphide bonds of the immunoglobulins was my own short-cut to the understanding of antibody diversity.
It now seems certain that the amino acid sequence of any protein is determined by the sequence of bases in some region of a particular nucleic acid molecule.
A comparison between the triplets tentatively deduced by these methods with the changes in amino acid sequence produced by mutation shows a fair measure of agreement.
This seems highly likely, especially as it has been shown that in several systems mutations affecting the same amino acid are extremely near together on the genetic map.
A final proof of our ideas can only be obtained by detailed studies on the alterations produced in the amino acid sequence of a protein by mutations of the type discussed here.
Unfortunately it makes the unambiguous determination of triplets by these methods much more difficult than would be the case if there were only one triplet for each amino acid.
It now seems very likely that many of the 64 triplets, possibly most of them, may code one amino acid or another, and that in general several distinct triplets may code one amino acid.
The balance of evidence both from the cell-free system and from the study of mutation, suggests that this does not occur at random, and that triplets coding the same amino acid may well be rather similar.
The meaning of this observation is unclear, but it raises the unfortunate possibility of ambiguous triplets; that is, triplets which may code more than one amino acid. However one would certainly expect such triplets to be in a minority.
That the primary effect of gene mutation may be as simple as the substitution of a single amino acid by another and may lead to profound secondary changes in protein structure and properties has recently been strongly indicated by the work of Ingram on hemoglobin.
Human insulin differs from other mammalian types by having a different C-terminal amino acid on the B chain. The immunological difference between beef insulin and human insulin, which is presumably responsible for the antigenicity of the former in some human beings, is thus limited to very a small portion of the whole molecule.