Biopolymers and cell. 2007; 23 (4): 307 - 317

Conformational mobility of human translation elongation factor A1

D. S. Kanibolotsky, A. V. Novosil'naya, B. S. Negrutskii, A. V. El'skaya

A model of the eEF1A1 isoform of human translation elongation factor 1A has been proposed using a homology modelling method. The conformational mobility of eEF1A1 has been studied by means of multiple molecular dynamics simulation. The most essential coordinated motions in the protein have been identified using the covariance analysis of atom trajectories. It has been determined that reciprocal flexibility of domains I and II can lead to disappearance of the gap between the domains and to formation of a «closed» conformation of the protein. The amino acid residues, which are characterised by maximal flexibility of C_α-atoms, have been described.

Keywords: protein synthesis, translation elongation, protein molecular dynamics.