Emergence of information transmission in a prebiotic RNA reactor

A poorly understood step in the transition from a chemical to a biological world is the emergence of self-replicating molecular systems. We study how a precursor for such a replicator might arise in a hydrothermal RNA reactor, which accumulates longer sequences from unbiased monomer influx and random ligation. In the reactor, intra- and intermolecular base pairing locally protects from random cleavage. By analyzing stochastic simulations, we find temporal sequence correlations that constitute a signature of information transmission, weaker but of the same form as in a true replicator.     

Zur Analyse der ätherischen Öle

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Über eine quantitative Reaction des Lignins

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UV Photolysis of a Re(I) Macromolecule, [(4-vinylpyridine)2(4-vinylpyridineRe(C0)3(1,10-phenanthroline)+]200: Addition of C-centered Radicals to Coordinated CO

Abstract

Proteins that bind preferentially to specific recognition sites on DNA also bind more weakly to nonspecific DNA. We have studied both specific and non-specific binding of the EcoRI and BamHI restriction endonucleases, and determined enthalpic and entropic contributions to binding free energy (ΔG°_bind) using both the van't Hoff method and isothermal titration calorimetry. Specific binding is characterized by a strongly negative ΔC°_p and can be either enthalpy-driven or entropy-driven, depending on temperature. Nonspecific binding has ΔC°_p ≈ 0 and is enthalpy-driven. A strongly negative ΔC°_p is the ?thermodynamic signature’ of site-specific binding, because it reflects the characteristics of a tight complementary recognition interface: the burial of previously hydrated nonpolar surface and restriction of configurational-vibrational freedoms of protein, DNA, and water molecules trapped at the protein-DNA interface. These factors are absent in nonspecific complexes. We probed the contributions to ΔC°_p by varying the sequence context surrounding the recognition site. As ΔG°_bind improves, ΔC°_p' ΔH° and ΔS° all become more negative, and there is a linear correlation between ΔH° and ΔS° (enthalpy-entropy compensation). Because these context variations do not change the protein-base or protein-phosphate contacts, the hydrophobic contribution or the number of trapped water molecules at the interface, we conclude that a better sequence context improves the ?goodness of fit’ in the interface and and thus increases the magnitude of the negative configurational-vibrational contribution to ΔC°_p.     

Über korrespondierende Punkte der Steinerschen Fläche vierter Ordnung und die Hauptpunkte derselben

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