/sci/ - Science & Math

>>15558232
>evolutionary history

The theory of evolution has been disproved
https://www.sciencedirect.com/science/article/abs/pii/0022519377900443

https://pubmed.ncbi.nlm.nih.gov/2199970/
>A method of targeted random mutagenesis has been used to investigate the informational content of 25 residue positions in two alpha-helical regions of the N-terminal domain of lambda repressor. Examination of the functionally allowed sequences indicates that there is a wide range in tolerance to amino acid substitution at these positions. At positions that are buried in the structure, there are severe limitations on the number and type of residues allowed. At most surface positions, many different residues and residue types are tolerated. However, at several surface positions there is a strong preference for hydrophilic amino acids, and at one surface position proline is absolutely conserved. The results reveal the high level of degeneracy in the information that specifies a particular protein fold.

This study was conducted at M.I.T where the authors experimented with re-building proteins by taking away amino acids and replacing them with other amino acids. They found that some parts of a protein chain are tolerant to substitutions but other parts are completely intolerant, showing that proteins are not arbitrary collections of component chemicals but rare and unique combinations. This confirm the conclusion of my first source that the probability of a specific folded protein coming into being by undirected evolution is 1 in 10(65). The practically infinite number of other combinations that could form at random are useless protein sequences for living organisms.

https://www.sciencedirect.com/science/article/abs/pii/0022519377900443

https://pubmed.ncbi.nlm.nih.gov/2199970/
>A method of targeted random mutagenesis has been used to investigate the informational content of 25 residue positions in two alpha-helical regions of the N-terminal domain of lambda repressor. Examination of the functionally allowed sequences indicates that there is a wide range in tolerance to amino acid substitution at these positions. At positions that are buried in the structure, there are severe limitations on the number and type of residues allowed. At most surface positions, many different residues and residue types are tolerated. However, at several surface positions there is a strong preference for hydrophilic amino acids, and at one surface position proline is absolutely conserved. The results reveal the high level of degeneracy in the information that specifies a particular protein fold.

This study was conducted at M.I.T where the authors experimented with re-building proteins by taking away amino acids and replacing them with other amino acids. They found that some parts of a protein chain are tolerant to substitutions but other parts are completely intolerant, showing that proteins are not arbitrary collections of component chemicals but rare and unique combinations. This confirm the conclusion of my first source that the probability of a specific folded protein coming into being by undirected evolution is 1 in 10(65). The practically infinite number of other combinations that could form at random are useless protein sequences for living organisms.