Anomalous dynamics of a lipid recognition protein on a membrane surface
Pleckstrin homology (PH) domains are lipid-binding modules present in peripheral membrane proteins which interact with phosphatidyl-inositol phosphates (PIPs) in cell membranes. We use multiscale molecular dynamics simulations to characterize the localization and anomalous dynamics of the DAPP1 PH d...
Glavni autori: | Yamamoto, E, Kalli, A, Akimoto, T, Yasuoka, K, Sansom, M |
---|---|
Format: | Journal article |
Izdano: |
Nature Publishing Group
2015
|
Slični predmeti
-
Dynamic interactions between a membrane binding protein and lipids induce fluctuating diffusivity
od: Yamamoto, E, i dr.
Izdano: (2017) -
Interactions of pleckstrin homology domains with membranes: adding back the bilayer via high throughput molecular dynamics
od: Yamamoto, E, i dr.
Izdano: (2016) -
Modes of interaction of pleckstrin homology domains with membranes: towards a computational biochemistry of membrane recognition
od: Naughton, F, i dr.
Izdano: (2017) -
Multiple lipid binding sites determine the affinity of PH domains for phosphoinositide-containing membranes
od: Domański, J, i dr.
Izdano: (2020) -
Association of peripheral membrane proteins with membranes: free energy of binding of GRP1 PH domain with phosphatidylinositol phosphate-containing model bilayers
od: Naughton, F, i dr.
Izdano: (2016)