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Microscopic Identification of PIP2 Binding Sites on a Ca2+-activated Cl- Channel
[chapter]
2021
Zenodo
Membrane proteins dwell in a sea of phospholipids that not only structurally stabilize the proteins by providing a hydrophobic environment but also dynamically regulate protein function. While many cation channels are known to be regulated by the negatively charged phosphatidylinositol 4,5-bisphosphate (PIP2), relatively little is known about anion channel regulation by phosphoinositides. Using atomistic molecular dynamics simulations on Blue Waters combined with experimental patch clamp
doi:10.5281/zenodo.4739640
fatcat:nkly42ccnjez5evotdvilmwgay