Investigation of the mechanical properties of immunoglobulinbinding domains of proteins L and G using the molecular dynamics simulations

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Mechanical unfolding of two identical in structure but differ in their amino acid sequences immunoglobulinbinding domains of proteins L and G under the action of external forces have been investigating  using the method of molecular dynamics with explicit model of solvent. Mechanical characteristics of these proteins have been calculated. It has been shown that in the way of the mechanical unfolding of both proteins appear intermediate states. Calculations revealed three significantly different ways of mechanical unfolding of proteins L and G.

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Citation in English: Glyakina A.V., Galzitskaya O.V., Balabaev N.K. Investigation of the mechanical properties of immunoglobulinbinding domains of proteins L and G using the molecular dynamics simulations // Computer Research and Modeling, 2010, vol. 2, no. 1, pp. 73-81
Citation in English: Glyakina A.V., Galzitskaya O.V., Balabaev N.K. Investigation of the mechanical properties of immunoglobulinbinding domains of proteins L and G using the molecular dynamics simulations // Computer Research and Modeling, 2010, vol. 2, no. 1, pp. 73-81
DOI: 10.20537/2076-7633-2010-2-1-73-81
According to Crossref, this article is cited by:
  • Ilya Viatcheslavovich Lihachev, Oksana V. Galzitskaya, Nikolai K. Balabaev. Investigation of C-Cadherin mechanical properties by Molecular Dynamics. // Computer Research and Modeling. 2013. — V. 5, no. 4. — P. 727. DOI: 10.20537/2076-7633-2013-5-4-727-735
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