by Shaun Doyle
Evolutionists have often claimed that gene duplication provides the raw material to produce new functions through subsequent mutation and natural selection. However, finding gene duplications that have produced new functions hasn’t been easy. Most gene duplications studied have been silenced and subjected to deleterious mutations, rendering them useless.1 However, a class of proteins called antifreeze proteins (AFPs) appear to have gone against this trend. AFPs are found in a wide variety of organisms: fish, insects, plants and microbes. They also take as many different forms as there are organisms that have them, and many are believed to have evolved via gene duplication events. These proteins bind to the surface of ice crystals and prevent water molecules from binding to the ice crystals, preventing the ice crystals from growing. This enables organisms to survive in sub-zero temperatures without freezing.
However, postulating that gene duplication and subsequent mutation can result in new functional proteins is not enough. To build a plausible case for neo-Darwinism one needs to identify the source of the new gene and outline the major mutations that actually lead to the change. Researchers have recently posited a detailed evolutionary scenario for the evolution of an antifreeze protein from such a gene duplication event in a species of Antarctic eelpout (ray-finned fish), Lycodichthys dearborni.2 So do these AFPs represent a neo-Darwinian mechanism producing a new protein? And if they are, what does this say for the plausibility of neo-Darwinism forming the mechanistic basis for microbes-to-man evolution?
The edge of eelpout evolution
Lycodichthys dearborni is one of several species of Antarctic eelpout of the family Zoarcidae. It is found in McMurdo Sound, south of the Ross Sea, off the coast of Antarctica. Zoarcids are one of only two families of fish to possess a particular class of AFPs, type III. The origin of type III AFPs has been particularly difficult for evolutionists to trace.3….
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