How and why kinetics, thermodynamics, and chemistry induce the logic of biological evolution.

Thermodynamic stability, as expressed by the Second Law, generally constitutes the driving force for chemical assembly processes. Yet, somehow, within the living world most self-organisation processes appear to challenge this fundamental rule. Even though the Second Law remains an inescapable constraint, under energy-fuelled, far-from-equilibrium conditions, populations of chemical systems capable of exponential growth can manifest another kind of stability, dynamic kinetic stability (DKS).

The Logic of Life.

In this paper we propose a logical connection between the physical and biological worlds, one resting on a broader understanding of the stability concept. We propose that stability manifests two facets - time and energy, and that stability's time facet, expressed as persistence, is more general than its energy facet. That insight leads to the logical formulation of the Persistence Principle, which describes the general direction of material change in the universe, and which can be stated most simply as: nature seeks persistent forms.

Stability and its manifestation in the chemical and biological worlds.

Bridging between the phenomenologically distinct biological and physical worlds has been a major scientific challenge since Boltzmann's probabilistic formulation of the second law of thermodynamics. In this review we summarize our recent theoretical attempts to bridge that divide through analysis of the thermodynamic-kinetic interplay in chemical processes and the manner in which that interplay impacts on material stability. Key findings are that the term 'stability' manifests two facets - time and energy - and that stability's time facet, expressed as persistence, is more general than its energy facet.

Evolutionary importance of the intramolecular pathways of hydrolysis of phosphate ester mixed anhydrides with amino acids and peptides.

Aminoacyl adenylates (aa-AMPs) constitute essential intermediates of protein biosynthesis. Their polymerization in aqueous solution has often been claimed as a potential route to abiotic peptides in spite of a highly efficient CO2-promoted pathway of hydrolysis. Here we investigate the efficiency and relevance of this frequently overlooked pathway from model amino acid phosphate mixed anhydrides including aa-AMPs.