PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 1710494-4 1991 Electron spin resonance (ESR) spectra of phosphatidylglycerol spin-labeled at position n = 5 in the sn-2 chain showed that complexation of MBP with the PLP-DMPG recombinants leads to a decrease in lipid chain mobility to an extent which correlates with the degree of MBP binding. dimyristoylphosphatidylglycerol 156-160 proteolipid protein 1 Bos taurus 152-155 1710494-1 1991 The integral proteolipid apoprotein (PLP) from bovine spinal cord has been reconstituted in dimyristoylphosphatidylglycerol (DMPG) bilayers, and the mutual interactions on binding the peripheral myelin basic protein (MBP) have been studied. dimyristoylphosphatidylglycerol 92-123 proteolipid protein 1 Bos taurus 37-40 1710494-1 1991 The integral proteolipid apoprotein (PLP) from bovine spinal cord has been reconstituted in dimyristoylphosphatidylglycerol (DMPG) bilayers, and the mutual interactions on binding the peripheral myelin basic protein (MBP) have been studied. dimyristoylphosphatidylglycerol 125-129 proteolipid protein 1 Bos taurus 37-40 1710494-2 1991 Quantitation of protein and lipid contents in the MBP-PLP-DMPG double recombinants at different PLP:DMPG ratios led to the conclusion that MBP binds only to the DMPG lipid headgroups and is hindered from interaction with the first shell of lipids surrounding the PLP. dimyristoylphosphatidylglycerol 58-62 proteolipid protein 1 Bos taurus 54-57 1710494-5 1991 At low DMPG:PLP ratios, the perturbations of lipid mobility by both proteins are mutually enhanced. dimyristoylphosphatidylglycerol 7-11 proteolipid protein 1 Bos taurus 12-15 1710494-6 1991 In single recombinants of PLP with DMPG, the ESR spectra of phosphatidylglycerol spin-labeled at position n = 14 in the sn-2 chain indicated that approximately 10 lipids/protein are motionally restricted by direct contact with the intramembranous surface of the protein. dimyristoylphosphatidylglycerol 35-39 proteolipid protein 1 Bos taurus 26-29 1710494-7 1991 This number is in agreement with earlier results for reconstitutions of PLP in dimyristoylphosphatidylcholine (DMPC) [Brophy, P. J., Horvath, L. I., & Marsh, D. (1984) Biochemistry 23, 860-865] and is consistent with a hexameric arrangement of the PLP molecules in DMPG bilayers. dimyristoylphosphatidylglycerol 269-273 proteolipid protein 1 Bos taurus 72-75