Selective and mutational constraints in the evolution of protein folding thermodynamics and kinetics

Ugo Bastolla

Universidad Autonoma de Madrid, Centro de Biologia Molecular, CSIC, Unidad de Bioinformatica, Madrid, Spain

I will discuss how the properties of protein folding thermodynamics and kinetics arise from the interplay between the mutation process (in particular, the mutation rate, mutation bias, and effective population size) and natural selection. I will illustrate this interplay through examples that show that protein folding thermodynamics correlates with genomic and population features, that selection for folding stability is stronger in short proteins, and selection for fast folding is stronger in long proteins, where it determines a peculiar pattern of strong and weak contacts.

Back