Conformational mobility of human translation elongation factor A1

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 iden...

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Bibliographic Details
Published inBiopolimery i kletka Vol. 23; no. 4; pp. 307 - 317
Main Authors Kanibolotsky, D. S., Novosil'naya, A. V., Negrutskii, B. S., El'skaya, A. V.
Format Journal Article
LanguageEnglish
Published Kiev Natsional'na Akademiya Nauk Ukrainy - National Academy of Sciences of Ukraine 2007
Subjects
Amino acids
eEF1A protein
Homology
Mobility
Molecular dynamics
Protein structure
Translation
Translation elongation
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Summary: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 C6-atoms, have been described.
ISSN:0233-7657
1993-6842
DOI:10.7124/bc.00076E