Cholesterol-dependent partitioning of PtdIns (4, 5) P2 into membrane domains by the N-terminal fragment of NAP-22 (neuronal axonal myristoylated membrane …
A myristoylated peptide corresponding to the N-terminus of NAP-22 (neuronal axonal
myristoylated membrane protein of 22 kDa) causes the quenching of the fluorescence of
BODIPY®-TMR-labelled PtdIns (4, 5) P 2 in bilayers of 1-palmitoyl-2-oleoyl
phosphatidylcholine containing 40 mol% cholesterol and 0.1 mol% BODIPY®–PtdIns (4, 5)
2. Both fluorescence spectroscopy and total internal reflectance fluorescence microscopy
revealed the cholesterol-dependent nature of PtdIns (4, 5) P 2-enriched membrane-domain …
myristoylated membrane protein of 22 kDa) causes the quenching of the fluorescence of
BODIPY®-TMR-labelled PtdIns (4, 5) P 2 in bilayers of 1-palmitoyl-2-oleoyl
phosphatidylcholine containing 40 mol% cholesterol and 0.1 mol% BODIPY®–PtdIns (4, 5)
2. Both fluorescence spectroscopy and total internal reflectance fluorescence microscopy
revealed the cholesterol-dependent nature of PtdIns (4, 5) P 2-enriched membrane-domain …
A myristoylated peptide corresponding to the N-terminus of NAP-22 (neuronal axonal myristoylated membrane protein of 22 kDa) causes the quenching of the fluorescence of BODIPY®-TMR-labelled PtdIns(4,5)P2 in bilayers of 1-palmitoyl-2-oleoyl phosphatidylcholine containing 40 mol% cholesterol and 0.1 mol% BODIPY®–PtdIns(4,5)2. Both fluorescence spectroscopy and total internal reflectance fluorescence microscopy revealed the cholesterol-dependent nature of PtdIns(4,5)P2-enriched membrane-domain formation.
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