A Quote by Francis Crick

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. — © Francis Crick
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.
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 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.
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.
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.
Attempts have been made from a study of the changes produced by mutation to obtain the relative order of the bases within various triplets, but my own view is that these are premature until there is more extensive and more reliable data on the composition of the triplets.
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 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.
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.
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.
What do we measure when we measure time? The gloomy answer from Hawking, one of our most implacably cheerful scientists, is that we measure entropy. We measure changes and those changes are all for the worse. We measure increasing disorder. Life is hard, says science, and constancy is the greatest of miracles.
The comparison between Coleridge and Johnson is obvious in so far as each held sway chiefly by the power of his tongue. The difference between their methods is so marked that it is tempting, but also unnecessary, to judge one to be inferior to the other. Johnson was robust, combative, and concrete; Coleridge was the opposite. The contrast was perhaps in his mind when he said of Johnson: "his bow-wow manner must have had a good deal to do with the effect produced.
Although random mutations influenced the course of evolution, their influence was mainly by loss, alteration, and refinement... Never, however, did that one mutation make a wing, a fruit, a woody stem, or a claw appear. Mutations, in summary, tend to induce sickness, death, or deficiencies. No evidence in the vast literature of heredity changes shows unambiguous evidence that random mutation itself, even with geographical isolation of populations, leads to speciation.
One amino acid does not a protein make-let alone a being.
People crave laughter as if it were an essential amino acid.
I take protein and amino acid supplements, but I honestly don't know if they do anything.
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.
This site uses cookies to ensure you get the best experience. More info...
Got it!