From Yahoo News:
The new research — which involves two studies, one led by Charles Carter and one led by Richard Wolfenden, both of the University of North Carolina — suggests a way for RNA to control the production of proteins by working with simple amino acids that does not require the more complex enzymes that exist today.
This link would bridge this gap in knowledge between the primordial chemical soup and the complex molecules needed to build life. Current theories say life on Earth started in an “RNA world,” in which the RNA molecule guided the formation of life, only later taking a backseat to DNA, which could more efficiently achieve the same end result. Like DNA, RNA is a helix-shaped molecule that can store or pass on information. (DNA is a double-stranded helix, whereas RNA is single-stranded.) Many scientists think the first RNA molecules existed in a primordial chemical soup — probably pools of water on the surface of Earth billions of years ago. More.
So this would support RNA World, the five-star hotel of origin-of-life theories
Physicist Rob Sheldon writes to note the remark,
We also looked at the structure of the autocatalytic sets our algorithm identified. Contrary to Kauffman’s original argument that autocatalytic sets emerge as a giant connected components, it turns out that autocatalytic sets can often be decomposed into smaller subsets, which themselves are autocatalytic. In fact, there often exists an entire hierarchy of smaller and smaller autocatalytic subsets. The smallest autocatalytic sets, which cannot be decomposed any further, are called irreducible autocatalytic sets.
In recent groundbreaking work, a group of researchers including Kauffman and Hungarian theoretical evolutionary biologist Eors Szathmary convincingly showed that autocatalytic sets composed of multiple small, irreducible subsets can, in fact, evolve. The main idea is that these autocatalytic subsets can exist in different combinations within a compartment (a protocell), thus giving rise to different types of protocells, and, consequently, to competition and selection. This, combined with our own results that one can indeed expect many such irreducible autocatalytic subsets to exist within a reaction network, suggests that autocatalytic sets are likely to arise from sufficiently complex chemical reaction networks and go on to evolve into larger and more complex systems.
Notice that “evolving” operates at the level of moving IC chess pieces.
Yes, we did notice the design assumptions and language. But naw, it all just sort of happened. 😉
Abstract The hydrophobicities of the 20 common amino acids are reflected in their tendencies to appear in interior positions in globular proteins and in deeply buried positions of membrane proteins. To determine whether these relationships might also have been valid in the warm surroundings where life may have originated, we examined the effect of temperature on the hydrophobicities of the amino acids as measured by the equilibrium constants for transfer of their side-chains from neutral solution to cyclohexane (Kw>c). The hydrophobicities of most amino acids were found to increase with increasing temperature. Because that effect is more pronounced for the more polar amino acids, the numerical range of Kw>c values decreases with increasing temperature. There are also modest changes in the ordering of the more polar amino acids. However, those changes are such that they would have tended to minimize the otherwise disruptive effects of a changing thermal environment on the evolution of protein structure. Earlier, the genetic code was found to be organized in such a way that—with a single exception (threonine)—the side-chain dichotomy polar/nonpolar matches the nucleic acid base dichotomy purine/pyrimidine at the second position of each coding triplet at 25 ̊C. That dichotomy is preserved at 100 ̊C. The accessible surface areas of amino acid side-chains in folded proteins are moderately correlated with hydrophobicity, but when free energies of vapor-to-cyclohexane transfer (corresponding to size) are taken into consideration, a closer relationship becomes apparent (paywall) .– Richard Wolfenden, Charles A. Lewis Jr., Yang Yuan, and Charles W. Carter Jr. Temperature dependence of amino acid hydrophobicities. Proceedings of the National Academy of Sciences, 2015; DOI: 10.1073/pnas.1507565112
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