PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 21117173-1 2010 The effect of PDC-109 binding to dimyristoylphosphatidylcholine (DMPC) and dipalmitoylphosphatidylglycerol (DPPG) multilamellar vesicles (MLVs) and supported membranes was investigated by (31)P NMR spectroscopy and atomic force microscopy. Dimyristoylphosphatidylcholine 33-63 seminal plasma protein PDC-109 Bos taurus 14-21 21117173-1 2010 The effect of PDC-109 binding to dimyristoylphosphatidylcholine (DMPC) and dipalmitoylphosphatidylglycerol (DPPG) multilamellar vesicles (MLVs) and supported membranes was investigated by (31)P NMR spectroscopy and atomic force microscopy. Dimyristoylphosphatidylcholine 65-69 seminal plasma protein PDC-109 Bos taurus 14-21 21117173-3 2010 Binding of PDC-109 to MLVs of DMPC and DPPG induced the formation of an isotropic signal in their (31)P NMR spectra, which increased with increasing protein/lipid ratio and temperature, consistent with protein-induced disruption of the MLVs and the formation of small unilamellar vesicles or micelles but not inverse hexagonal or cubic phases. Dimyristoylphosphatidylcholine 30-34 seminal plasma protein PDC-109 Bos taurus 11-18 19683598-2 2009 The increase in the intrinsic fluorescence emission intensity of PDC-109/B upon binding to lysophosphatidylcholine (Lyso-PC) micelles and dimyristoylphosphatidylcholine (DMPC) membranes was considerably less as compared to that observed with the whole PDC-109 protein. Dimyristoylphosphatidylcholine 138-168 seminal plasma protein PDC-109 Bos taurus 65-74 19683598-2 2009 The increase in the intrinsic fluorescence emission intensity of PDC-109/B upon binding to lysophosphatidylcholine (Lyso-PC) micelles and dimyristoylphosphatidylcholine (DMPC) membranes was considerably less as compared to that observed with the whole PDC-109 protein. Dimyristoylphosphatidylcholine 138-168 seminal plasma protein PDC-109 Bos taurus 65-72 19683598-2 2009 The increase in the intrinsic fluorescence emission intensity of PDC-109/B upon binding to lysophosphatidylcholine (Lyso-PC) micelles and dimyristoylphosphatidylcholine (DMPC) membranes was considerably less as compared to that observed with the whole PDC-109 protein. Dimyristoylphosphatidylcholine 170-174 seminal plasma protein PDC-109 Bos taurus 65-74 19683598-2 2009 The increase in the intrinsic fluorescence emission intensity of PDC-109/B upon binding to lysophosphatidylcholine (Lyso-PC) micelles and dimyristoylphosphatidylcholine (DMPC) membranes was considerably less as compared to that observed with the whole PDC-109 protein. Dimyristoylphosphatidylcholine 170-174 seminal plasma protein PDC-109 Bos taurus 65-72 19683598-3 2009 The degree of quenching achieved by different quenchers with PDC-109/B bound to Lyso-PC and DMPC membranes was significantly higher as compared to the full PDC-109 protein, indicating that membrane binding afforded considerably lesser protection to the tryptophan residues of domain B as compared to those in the full PDC-109 protein. Dimyristoylphosphatidylcholine 92-96 seminal plasma protein PDC-109 Bos taurus 61-70 19683598-3 2009 The degree of quenching achieved by different quenchers with PDC-109/B bound to Lyso-PC and DMPC membranes was significantly higher as compared to the full PDC-109 protein, indicating that membrane binding afforded considerably lesser protection to the tryptophan residues of domain B as compared to those in the full PDC-109 protein. Dimyristoylphosphatidylcholine 92-96 seminal plasma protein PDC-109 Bos taurus 61-68 19683598-4 2009 Finally, changes in red-edge excitation shift (REES) seen with PDC-109/B upon binding to DMPC membranes and Lyso-PC micelles were smaller that the corresponding changes in the REES values observed for the full PDC-109. Dimyristoylphosphatidylcholine 89-93 seminal plasma protein PDC-109 Bos taurus 63-72 19683598-4 2009 Finally, changes in red-edge excitation shift (REES) seen with PDC-109/B upon binding to DMPC membranes and Lyso-PC micelles were smaller that the corresponding changes in the REES values observed for the full PDC-109. Dimyristoylphosphatidylcholine 89-93 seminal plasma protein PDC-109 Bos taurus 63-70 18402784-7 2008 Upon binding of PDC-109 to DMPC membranes and Lyso-PC micelles the REES values were reduced to 2.5 and 1.0 nm, respectively, which could be due to the penetration of some parts of the protein, especially the segment containing Trp-90 into the membrane interior, where the red-edge effects are considerably reduced. Dimyristoylphosphatidylcholine 27-31 seminal plasma protein PDC-109 Bos taurus 16-23 12719234-6 2003 The dissociation rate constant (k(-1)) for the DMPC/PDC-109 system was found to be 2.7 x 10(-2) s(-1) whereas the k(-1) values obtained with DMPG and DMPA was about three to four times higher. Dimyristoylphosphatidylcholine 47-51 seminal plasma protein PDC-109 Bos taurus 52-59 12719234-7 2003 From the kinetic data, the association constant for the binding of PDC-109 to DMPC was estimated as 2.1 x 10(7) M(-1). Dimyristoylphosphatidylcholine 78-82 seminal plasma protein PDC-109 Bos taurus 67-74 12719234-9 2003 Thus the higher affinity of PDC-109 for choline phospholipids is reflected in a faster association rate constant and a slower dissociation rate constant for DMPC as compared to the other phospholipids. Dimyristoylphosphatidylcholine 157-161 seminal plasma protein PDC-109 Bos taurus 28-35 12719234-11 2003 Analysis of the activation parameters indicates that the interaction of PDC-109 with DMPC membranes is favored by a strong entropic contribution, whereas negative entropic contribution is primarily responsible for the rather weak interaction of this protein with DMPA and DMPG. Dimyristoylphosphatidylcholine 85-89 seminal plasma protein PDC-109 Bos taurus 72-79 12297311-2 2002 The selectivity of PDC-109 for different spin-labelled phospholipids and sterol probes in dimyristoylphosphatidylcholine (DMPC) host matrix has been characterized earlier by EPR spectroscopy [Ramakrishnan, M., Anbazhagan, V., Pratap, T.V., Marsh, D. and Swamy, M.J. (2001) Biophys. Dimyristoylphosphatidylcholine 90-120 seminal plasma protein PDC-109 Bos taurus 19-26 12297311-2 2002 The selectivity of PDC-109 for different spin-labelled phospholipids and sterol probes in dimyristoylphosphatidylcholine (DMPC) host matrix has been characterized earlier by EPR spectroscopy [Ramakrishnan, M., Anbazhagan, V., Pratap, T.V., Marsh, D. and Swamy, M.J. (2001) Biophys. Dimyristoylphosphatidylcholine 122-126 seminal plasma protein PDC-109 Bos taurus 19-26 12297311-5 2002 In this report the effect of cholesterol on the interaction of PDC-109 with DMPC membranes has been investigated by spin-label EPR spectroscopy. Dimyristoylphosphatidylcholine 76-80 seminal plasma protein PDC-109 Bos taurus 63-70 21408153-6 2011 Presence of DMPC was found to increase the CLA of PDC-109 significantly, which could be due to the considerable exposure of hydrophobic regions on the lipid-protein recombinants, which can interact productively with the nonnative structures of target proteins, resulting in their protection. Dimyristoylphosphatidylcholine 12-16 seminal plasma protein PDC-109 Bos taurus 50-57 21408153-8 2011 Cholesterol incorporation into DMPC membranes led to a decrease in the CLA of PDC-109-lipid recombinants, which could be attributed to reduced accessibility of hydrophobic surfaces to the substrate protein(s). Dimyristoylphosphatidylcholine 31-35 seminal plasma protein PDC-109 Bos taurus 78-85 22022488-5 2011 Binding of PDC-109 with dimyristoylphosphatidylcholine membranes containing 25 mol% cholesterol showed an initial increase in the association constant as well as enthalpy and entropy of binding with increase in temperature, whereas the values decreased with further increase in temperature. Dimyristoylphosphatidylcholine 24-54 seminal plasma protein PDC-109 Bos taurus 11-18 11566792-1 2001 The interaction of the major acidic bovine seminal plasma protein, PDC-109, with dimyristoylphosphatidylcholine (DMPC) membranes has been investigated by spin-label electron spin resonance spectroscopy. Dimyristoylphosphatidylcholine 81-111 seminal plasma protein PDC-109 Bos taurus 43-74 11566792-1 2001 The interaction of the major acidic bovine seminal plasma protein, PDC-109, with dimyristoylphosphatidylcholine (DMPC) membranes has been investigated by spin-label electron spin resonance spectroscopy. Dimyristoylphosphatidylcholine 113-117 seminal plasma protein PDC-109 Bos taurus 43-74 11566792-3 2001 Binding of PDC-109 at high protein/lipid ratios (PDC-109:DMPC = 1:2, w/w) results in a considerable decrease in the chain segmental mobility of the lipid as seen by spin-label electron spin resonance spectroscopy. Dimyristoylphosphatidylcholine 57-61 seminal plasma protein PDC-109 Bos taurus 11-18 11566792-4 2001 A further interesting new observation is that, at high concentrations, PDC-109 is capable of (partially) solubilizing DMPC bilayers. Dimyristoylphosphatidylcholine 118-122 seminal plasma protein PDC-109 Bos taurus 71-78 11566792-5 2001 The selectivity of PDC-109 in its interaction with membrane lipids was investigated by using different spin-labeled phospholipid and steroid probes in the DMPC host membrane. Dimyristoylphosphatidylcholine 155-159 seminal plasma protein PDC-109 Bos taurus 19-26