Explicit simulations of protein evolution, where protein chains are described at a molecular, although simplified, level provide important information to understand the similarities found to exist between known proteins. The results of such simulations suggest that a number of evolutionary-related quantities, such as the distribution of sequence similarity for structurally similar proteins, are controlled by evolutionary kinetics and do not reflect an equilibrium state. An important result for phylogeny is that a subset of the residues of each protein evolve on a much larger time scale than the other residues.

The evolution dynamics of model proteins / G. Tiana, N. V. Dokholyan, R. A. Broglia, E. I. Shakhnovich. - In: THE JOURNAL OF CHEMICAL PHYSICS. - ISSN 0021-9606. - 121:5(2004), pp. 2381-2389.

The evolution dynamics of model proteins

G. Tiana
Primo
;
R. A. Broglia
Penultimo
;
2004

Abstract

Explicit simulations of protein evolution, where protein chains are described at a molecular, although simplified, level provide important information to understand the similarities found to exist between known proteins. The results of such simulations suggest that a number of evolutionary-related quantities, such as the distribution of sequence similarity for structurally similar proteins, are controlled by evolutionary kinetics and do not reflect an equilibrium state. An important result for phylogeny is that a subset of the residues of each protein evolve on a much larger time scale than the other residues.
Settore FIS/03 - Fisica della Materia
2004
Article (author)
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/141269
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