Molecular dynamics of human alpha-fetoprotein fragment LDSYQCT and its analogs at different dielectric constants |
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Authors: | N. T. Moldogazieva K. V. Shaitan K. B. Tereshkina Yu. M. Antonov A. A. Terentiev |
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Affiliation: | (1) State Medical University, Moscow, 117997, Russia;(2) Faculty of Bioengineering, Moscow State University, Moscow, 119992, Russia |
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Abstract: | A comparative study of the conformation dynamics of the human alpha-fetoprotein fragment LDSYQCT and heptapeptides derived from it by point substitutions has revealed a significant influence of electrostatic interactions on the set of preferred conformations and dynamics of amino acid residues when the peptides with blocked termini are examined at ? = 1. Peptide flexibility rises when the termini are left free (charged). At ? = 10 or 80, the set of probable conformations for all residues expands to much the same extent, i.e., at higher permittivity of the medium the dynamic effects of amino acid changes are leveled off. |
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Keywords: | molecular dynamics simulation AFP oligopeptides point substitution electrostatic interactions dielectric permittivity |
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