Molecular dimension explored in evolution to promote proteomic complexity
AUTOR(ES)
Fernández, Ariel
FONTE
National Academy of Sciences
RESUMO
The architecture of present-day protein interaction networks depends on how protein associations evolved. Here, we explore how and why evolution-related mutations influence protein structure to promote protein associations, and thereby network development. We specifically address two questions: (i) How can protein folds remain conserved while proteins accommodate new binding partnerships as genes duplicate? (ii) What is the structural/molecular basis for hub proteins being the most likely to acquire new connections? The answers stem from the examination of the structure wrapping, or protection from water attack. Wrapping is shown to be a crucial consideration in the exploration and evolution of proteomic interactivity.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=518779Documentos Relacionados
- Evolution of biological complexity
- Molecular phylogeny analysis of fiddler crabs: test of the hypothesis of increasing behavioral complexity in evolution.
- Intrasexual selection predicts the evolution of signal complexity in lizards.
- Quantitative evaluation and modeling of two-dimensional neovascular network complexity: the surface fractal dimension
- A neo-Darwinian algorithm: asymmetrical mutations due to semiconservative DNA-type replication promote evolution.