Title : Steered molecular dynamics simulations on the "tail helix latch" hypothesis in the gelsolin activation process.

Pub. Date : 2002 Aug

PMID : 12124262






2 Functional Relationships(s)
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1 The subsequent simulation on Arg-207-Ala (R207A) mutation of gelsolin indicated that this mutation facilitates the unbinding of the tail helix and that the contribution of the hydrogen bond between Arg-207 and Asp-744 to the binding is more than 50%, which offers a new clue for further mutagenesis study on the activation mechanism of gelsolin. Aspartic Acid gelsolin Homo sapiens
2 The subsequent simulation on Arg-207-Ala (R207A) mutation of gelsolin indicated that this mutation facilitates the unbinding of the tail helix and that the contribution of the hydrogen bond between Arg-207 and Asp-744 to the binding is more than 50%, which offers a new clue for further mutagenesis study on the activation mechanism of gelsolin. Aspartic Acid gelsolin Homo sapiens