Computer simulations of prebiotic evolution.
This paper is a review of our previous work on the field of possible ways of prebiotic evolution. We propose an algorithm providing sequences of model proteins with rapid folding into a given native conformation. Thermodynamical analysis shows that the increase in speed is matched by an increase in stability: the evolved sequences are much more stable in their native conformation than the initial random sequence. We discuss a possible origin of the first biopolymers, having stable unique structure. We suggest that at the prebiotic stage of evolution, long organic polymers had to be compact in order to avoid hydrolysis and had to be soluble and thus must not be exceedingly hydrophobic. We present an algorithm that generates such sequences of model proteins. The evolved sequences turn out to have a stable unique structure, into which they quickly fold. This result illustrates the idea that the unique three-dimensional native structure of first biopolymers could have evolved as a side effect of a nonspecific physico-chemical factors acting at the prebiotic stage of evolution.
Abkevich
V I
VI
Harvard University, Department of Chemistry, Cambridge, MA 02138, USA.
Gutin
A M
AM
Shakhnovich
E I
EI
D000465:Algorithms; D005075:Biological Evolution; D003198:Computer Simulation; D008954:Models, Biological; D008958:Models, Molecular; D009154:Mutation; D000069497:Origin of Life; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry / Q000235:genetics; D011897:Random Allocation; D012984:Software; D013816:Thermodynamics
D011506:Proteins