Researchers just announced the systematic laboratory induced mutation of successive amino acids over the entire sequence of a simple bacterial protein.1 The results showed how even the simplest of life’s proteins have irreducibly complex chemical structures. The research also showed how random evolutionary processes that are ascribed to mutations are unable to propel evolution.
DNA holds the coded information that cells use to produce proteins, which are ordered chains of amino acids. Three successive nucleotide bases of DNA code for a single amino acid of a protein. Publishing in Nature, researchers successively changed the DNA code of an entire bacterial gene to mutate every amino acid of an 83-amino-acid protein. They then tested the ability of each mutant protein version to interact with its biological target in the cell.
What they proved was that proteins have a variety of specific regions that are highly sensitive to mutation—meaning that changes in these amino acids are not tolerated. Instead, they destroy protein function and negate evolution. These results support the prior research of Douglass Axe, a famous Cambridge protein biochemist who has also mutated large segments of bacterial proteins and is a strong critic of protein evolution and defender of intelligent design principles.2,3
In the simple bacterial protein they tested, 20 out of the 83 amino acids were off-limits to so-called random mutational evolutionary processes, since each of these single amino acid changes disabled protein function. Many of these mutation-resistant amino acid positions were in key sectors of the protein that interact with its “ligand, or chemical binding partner. Unfortunately for evolutionary concepts, these sectors are exactly where nature would need mutations to occur in order for it to construct new cellular interactions that might contribute to a new, selectable trait….
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