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Título : An Analysis of Core Deformations in Protein Superfamilies
Autor : Leo-Macías, Alejandra ; López-Romero, Pedro; Lupyan, Dmitry; Zerbino, Daniel; Ortiz, Ángel R.
Palabras clave : Protein superfamilies
Fecha de publicación : 12-nov-2004
Editor: Biophysical Society
Citación : Biophysical Journal 88:1291-1299 (2005)
Resumen: An analysis is presented on how structural cores modify their shape across homologous proteins, and whether or not a relationship exists between these structural changes and the vibrational normal modes that proteins experience as a result of the topological constraints imposed by the fold. A set of 35 representative, well-populated protein families is studied. The evolutionary directions of deformation are obtained by using multiple structural alignments to superimpose the structures and extract a conserved core, together with principal components analysis to extract the main deformation modes from the three-dimensional superimposition. In parallel, a low-resolution normal mode analysis technique is employed to study the properties of the mechanical core plasticity of these same families. We show that the evolutionary deformations span a low dimensional space of 4–5 dimensions on average. A statistically significant correspondence exists between these principal deformations and the 20 slowest vibrational modes accessible to a particular topology. We conclude that, to a significant extent, the structural response of a protein topology to sequence changes takes place by means of collective deformations along combinations of a small number of low-frequency modes. The findings have implications in structure prediction by homology modeling.
Versión del editor: http://www.biophysj.org/cgi/content/abstract/biophysj.104.052449v1
URI : http://hdl.handle.net/10261/8022
ISSN: 0006-3495 (print)
1542-0086 (online)
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