IndraLab

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sparser
"We next analyzed three states of IKK2: unphosphorylated (UnP-IKK2), phosphorylated at S177 and S181 (p-IKK2), and phosphorylated at Y169, S177, and S181 (P-IKK2) using computational approaches of molecular dynamic (MD) simulations of 200 ns scale and flexible molecular docking (see methods)."

sparser
"The results indicated that ATP binding to P-IKK2 is relatively unfavorable (docking score in positive range) in both starting and ending structural models ( xref ), whereas ATP binding to UnP-IKK2 and p-IKK2 is favorable."

sparser
"Counter-intuitively, we observed the highest RMSD for P-IKK2, followed by p-IKK2, and then UnP-IKK2 ( xref )."

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