Dynamic interactions between a membrane binding protein and lipids induce fluctuating diffusivity
Pleckstrin homology (PH) domains are membrane-binding lipid recognition proteins which interact with phosphatidyl-inositol-phosphate (PIP) molecules in eukaryotic cell membranes. Diffusion of PH domains plays a critical role in biological reactions on the membrane surfaces. Although diffusivity can...
Asıl Yazarlar: | Yamamoto, E, Akimoto, T, Kalli, A, Yasuoka, K, Sansom, M |
---|---|
Materyal Türü: | Journal article |
Baskı/Yayın Bilgisi: |
American Association for the Advancement of Science
2017
|
Benzer Materyaller
-
Anomalous dynamics of a lipid recognition protein on a membrane surface
Yazar:: Yamamoto, E, ve diğerleri
Baskı/Yayın Bilgisi: (2015) -
Interactions of pleckstrin homology domains with membranes: adding back the bilayer via high throughput molecular dynamics
Yazar:: Yamamoto, E, ve diğerleri
Baskı/Yayın Bilgisi: (2016) -
Multiple lipid binding sites determine the affinity of PH domains for phosphoinositide-containing membranes
Yazar:: Domański, J, ve diğerleri
Baskı/Yayın Bilgisi: (2020) -
Association of peripheral membrane proteins with membranes: free energy of binding of GRP1 PH domain with phosphatidylinositol phosphate-containing model bilayers
Yazar:: Naughton, F, ve diğerleri
Baskı/Yayın Bilgisi: (2016) -
Lipid/protein interactions and the membrane/water interfacial region.
Yazar:: Domene, C, ve diğerleri
Baskı/Yayın Bilgisi: (2003)