REC
Posts: 638
Joined: Sep. 2006
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VJtorley has spewed out a list of 12 fallacies scientists apparently commit. But, is there one for a philosopher faking a study of a scientific field, and bullshitting his way through?
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For the first claim, the evolutionists argue for a smaller protein sequence space because:
A. “the actual identity of most of the amino acids in a protein is irrelevant” and so we can assume there were only a few amino acids in the evolution of proteins, rather than today’s 20.
B. Only the surface residues of a protein are important.
C. Proteins need not be very long. Instead of hundreds of residues, evolution could have used about 50 for most proteins.
For Point A, the evolutionists use as support a series of simplistic studies that replaced the actual protein three-dimensional structure and amino acid chemistries with cartoon, two-dimensional lattice versions.…
Likewise Point B is at odds with science, and again is an unwarranted extrapolation on a simplistic lattice study.
For Point C, the evolutionists note that many proteins are modular and consist of self-contained domains “of as few as approximately 50 amino acids.” But the vast majority of protein domains are far longer than 50 residues. Single domain proteins, and domains in multiple-domain proteins are typically in the hundreds of residues…
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Point A: What does this phrase "two dimensional lattice" even mean? The scientists made, expressed, purified, and studied real (three dimensional) proteins with a reduced amino acid complement. They fold and function. e.g.:
Muller, M. et al. Directed Evolution of a Model Primordial Enzyme Provides Insights into the Development of the Genetic Code. PLOS Genetics, 2013, 9: e1003187, doi: 10.1371/journal.pgen.1003187
Point B: "Lattice study" again. He's simply made this up. Making real proteins with simplified hydrophobic cores was a popular trick. Pretty easy. Even ID hero Douglas Axe did it:
"These results imply that hydrophobicity is nearly a sufficient criterion for the construction of a functional core and, in conjunction with previous studies, that refinement of a crudely functional core entails more stringent sequence constraints than does the initial attainment of crude core function. Since attainment of crude function is the critical initial step in evolutionary innovation, the relatively scant requirements contributed by the hydrophobic core would greatly reduce the initial hurdle on the evolutionary pathway to novel enzymes."
http://www.ncbi.nlm.nih.gov/pubmed....8643620
Funny he ignores that study of his!!! In all honesty, if he disbelieves this data, he should retract. Or include the "reduce the initial hurdle" bit it in his big big numbers scam.
Point C: Vast majority are far longer than 50 residues? A single domain protein is ~4X more likely to be 50 amino acids long than 200 amino acids. The distribution of domain length peaks at ~100 amino acids and falls off pretty rapidly. Sorry, the data (in public databases) just doesn't support you. See figure 2:
http://bioinformatics.oxfordjournals.org/content....ull.pdf
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