Title : Neutron Scattering Studies of the Interplay of Amyloid β Peptide(1-40) and An Anionic Lipid 1,2-dimyristoyl-sn-glycero-3-phosphoglycerol.

Pub. Date : 2016 Aug 9

PMID : 27503057






3 Functional Relationships(s)
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1 In this work, we applied an array of neutron scattering methods to study the structure and dynamics of Abeta(1-40) interacting 1,2-dimyristoyl-sn-glycero-3-phosphoglycerol (DMPG) bilayers. dimyristoylphosphatidylglycerol amyloid beta precursor protein Homo sapiens
2 In the structural investigations of lipid bilayer"s response to Abeta binding, Small Angle Neutron Scattering and Neutron Membrane Diffraction revealed that the Abeta anchors firmly to the highly charged DMPG bilayers in the interfacial region between water and hydrocarbon chain, and it doesn"t penetrate deeply into the bilayer. dimyristoylphosphatidylglycerol amyloid beta precursor protein Homo sapiens
3 In the structural investigations of lipid bilayer"s response to Abeta binding, Small Angle Neutron Scattering and Neutron Membrane Diffraction revealed that the Abeta anchors firmly to the highly charged DMPG bilayers in the interfacial region between water and hydrocarbon chain, and it doesn"t penetrate deeply into the bilayer. dimyristoylphosphatidylglycerol amyloid beta precursor protein Homo sapiens