A hierarchical approach to protein molecular evolution
AUTOR(ES)
Bogarad, Leonard D.
FONTE
The National Academy of Sciences
RESUMO
Biological diversity has evolved despite the essentially infinite complexity of protein sequence space. We present a hierarchical approach to the efficient searching of this space and quantify the evolutionary potential of our approach with Monte Carlo simulations. These simulations demonstrate that nonhomologous juxtaposition of encoded structure is the rate-limiting step in the production of new tertiary protein folds. Nonhomologous “swapping” of low-energy secondary structures increased the binding constant of a simulated protein by ≈107 relative to base substitution alone. Applications of our approach include the generation of new protein folds and modeling the molecular evolution of disease.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=15812Documentos Relacionados
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