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A visual and Excel-based review of the Merton model used to estimate EDF (or probability of default). This is a structural approach; i.e,. default is predicted by the firm's balance sheet properties
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Just Folding One Single Protein Molecule, of which your body has countless trillions, would take a few hundred thousand computers weeks to accomplish. -
Evolution vs. Functional Proteins - Doug Axe - Video
In real life, the protein folds into its final shape in a fraction of a second! The Blue Gene computer would have to operate at least 33 million times faster to accomplish what the protein does in a fraction of a second. This is the complexity found for JUST ONE simple protein molecule. Yet, evolution must account for the origination of far, far, more than just one specifically sequenced protein molecule:
A New Guide to Exploring the Protein Universe
"It is estimated, based on the total number of known life forms on Earth, that there are some 50 billion different types of proteins in existence today, and it is possible that the protein universe could hold many trillions more."
Lynn Yarris - 2005
Michael Behe Talks About The Probability of A Single Protein - video
Origin Of Life? Where Does The Evidence Lead? - video
What makes matters much worse for the materialist is that he will try to assert proteins of one structure can easily mutate into other proteins, of a completely different structure, by pure chance. Yet once again the empirical evidence we now have brutally betrays the materialist. Individual proteins have been experimentally shown to quickly lose their structural integrity with random point mutations. What are the odds of any "functional protein domain" in a cell mutating into any other functional protein domain, of very questionable value, by pure chance?
Estimating the prevalence of protein sequences adopting functional enzyme folds: Doug Axe:
Excerpt: Starting with a weakly functional sequence carrying this signature, clusters of ten side-chains within the fold are replaced randomly, within the boundaries of the signature, and tested for function. The prevalence of low-level function in four such experiments indicates that roughly one in 10^64 signature-consistent sequences forms a working domain. Combined with the estimated prevalence of plausible hydropathic patterns (for any fold) and of relevant folds for particular functions, this implies the overall prevalence of sequences performing a specific function by any domain-sized fold may be as low as 1 in 10^77, adding to the body of evidence that functional folds require highly extraordinary sequences. (of note: the universe only has 10^80 sub-atomic particles)
Axe Diagram for finding a functional protein domain out of all sequence space:
The y-axis can be seen as representing enzyme activity, and the x-axis represents all possible amino acid sequences. Enzymes sit at the peak of their fitness landscapes (Point A). There are extremely high levels of complex and specified information in proteins--informational sequences which point to intelligent design.
Experimental Support for Regarding Functional Classes of Proteins to be Highly Isolated from Each Other:
"From actual experimental results it can easily be calculated that the odds of finding a folded protein (by random point mutations to an existing protein) are about 1 in 10 to the 65 power (Sauer, MIT). To put this fantastic number in perspective imagine that someone hid a grain of sand, marked with a tiny 'X', somewhere in the Sahara Desert. After wandering blindfolded for several years in the desert you reach down, pick up a grain of sand, take off your blindfold, and find it has a tiny 'X'. Suspicious, you give the grain of sand to someone to hide again, again you wander blindfolded into the desert, bend down, and the grain you pick up again has an 'X'. A third time you repeat this action and a third time you find the marked grain. The odds of finding that marked grain of sand in the Sahara Desert three times in a row are about the same as finding one new functional protein structure (from chance transmutation of an existing functional protein structure). Rather than accept the result as a lucky coincidence, most people would be certain that the game had been fixed. Michael J. Behe, The Weekly Standard, June 7, 1999
Intelligent Design - The Anthropic Hypothesis
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