Related ArticlesInteraction of myelin basic protein with single bilayers on a solid support: an NMR, DSC and polarized infrared ATR study.
Biochim Biophys Acta. 1993 Sep 19;1151(2):127-36
Authors: Reinl HM, Bayerl TM
The interaction of myelin basic protein (MBP) with single bilayers on a solid support (planar and spherical support) is studied by deuterium nuclear magnetic resonance (2H-NMR), differential scanning calorimetry (DSC) and polarized attenuated total reflection infrared spectroscopy (ATR-IR). The single bilayer consisted of either DMPC or of a binary mixture of DMPC with 10-20 mol% of an acidic phospholipid (DMPG, DMPS or DMPA). All methods applied indicate that MBP strongly interacts with the binary lipid systems but not with the pure DMPC bilayers. The interaction is predominantly electrostatic in nature and does not depend on the choice of a particular acidic lipid (for the binary systems). In particular, the results give no indication for a hydrophobic interaction of MBP with the membrane. Our data provide evidence that, in contrast to previous findings, no demixing and/or domain formation in the binary systems is induced due to the MBP coupling. The infrared order parameter was determined for both lipid components of the binary systems and shows a remarkable change for both lipids due to the interaction with MBP while the NMR order parameter remained essentially unchanged. This is discussed in terms of the different timescales characteristic for both methods. The single supported bilayer responds to the MBP coupling as a whole although only 50% of the bilayer surface is accessible to the protein, indicating a strong coupling between the two bilayer leaflets via the hydrophobic chain region. Moreover, the asymmetric coupling of MBP to the single supported bilayer does not result in a significant redistribution of lipids between the two bilayer leaflets. NMR relaxation time measurements in the headgroup and chain region of DMPG and DMPC suggest that the lateral diffusion coefficient of the acidic lipid decreases significantly due to the coupling with MBP while the zwitterionic DMPC is not affected.
[NMR paper] Solid-state NMR measurements of the kinetics of the interaction between phospholamban and Ca2+-ATPase in lipid bilayers.
Solid-state NMR measurements of the kinetics of the interaction between phospholamban and Ca2+-ATPase in lipid bilayers.
Related Articles Solid-state NMR measurements of the kinetics of the interaction between phospholamban and Ca2+-ATPase in lipid bilayers.
Mol Membr Biol. 2005 Jul-Aug;22(4):353-61
Authors: Hughes E, Middleton DA
Phospholamban (PLB) is a small transmembrane protein that regulates calcium transport across the sarcoplasmic reticulum (SR) of cardiac cells via a reversible inhibitory interaction with Ca2+-ATPase. In this work...
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[NMR paper] Investigation of the interaction of myelin basic protein with phospholipid bilayers u
Investigation of the interaction of myelin basic protein with phospholipid bilayers using solid-state NMR spectroscopy.
Related Articles Investigation of the interaction of myelin basic protein with phospholipid bilayers using solid-state NMR spectroscopy.
Chem Phys Lipids. 2004 Nov;132(1):47-54
Authors: Pointer-Keenan CD, Lee DK, Hallok K, Tan A, Zand R, Ramamoorthy A
Interaction of bovine myelin basic protein and its constituent charge isomers (C1-C3) with phospholipid bilayers was studied using solid-state NMR experiments on model...
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[NMR paper] NMR and molecular dynamics studies of an autoimmune myelin basic protein peptide and
NMR and molecular dynamics studies of an autoimmune myelin basic protein peptide and its antagonist: structural implications for the MHC II (I-Au)-peptide complex from docking calculations.
Related Articles NMR and molecular dynamics studies of an autoimmune myelin basic protein peptide and its antagonist: structural implications for the MHC II (I-Au)-peptide complex from docking calculations.
Eur J Biochem. 2004 Aug;271(16):3399-413
Authors: Tzakos AG, Fuchs P, van Nuland NA, Troganis A, Tselios T, Deraos S, Matsoukas J, Gerothanassis IP, Bonvin AM
...
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[NMR paper] Interaction of chicken liver basic fatty acid-binding protein with fatty acids: a 13C
Interaction of chicken liver basic fatty acid-binding protein with fatty acids: a 13C NMR and fluorescence study.
Related Articles Interaction of chicken liver basic fatty acid-binding protein with fatty acids: a 13C NMR and fluorescence study.
Biochemistry. 2001 Oct 23;40(42):12604-11
Authors: Beringhelli T, Goldoni L, Capaldi S, Bossi A, Perduca M, Monaco HL
Two different groups of liver fatty acid-binding proteins (L-FABPs) are known: the mammalian type and the basic type. Very few members of this second group of L-FABPs have been...
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Lipid-Protein Correlations in Nanoscale Phospholipid Bilayers by Solid-State NMR.
Lipid-Protein Correlations in Nanoscale Phospholipid Bilayers by Solid-State NMR.
Lipid-Protein Correlations in Nanoscale Phospholipid Bilayers by Solid-State NMR.
Biochemistry. 2010 Aug 30;
Authors: Kijac A, Shih AY, Nieuwkoop AJ, Schulten K, Sligar SG, Rienstra CM
Nanodiscs are an example of discoidal nanoscale lipid/protein particles that have been extremely useful for the biochemical and biophysical characterization of membrane proteins. They are discoidal lipid bilayer fragments encircled and stabilized by two amphipathic helical...
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[NMR paper] Proton NMR study of peptides from myelin basic protein: evidence for Lys74-His77 inte
Proton NMR study of peptides from myelin basic protein: evidence for Lys74-His77 interaction revealed from histidine line broadening.
Related Articles Proton NMR study of peptides from myelin basic protein: evidence for Lys74-His77 interaction revealed from histidine line broadening.
Biochim Biophys Acta. 1996 Mar 7;1293(1):23-30
Authors: Koshy KM, Hashim GA, Boggs JM
Residues 69-84 of guinea pig myelin basic protein contain the encephalitogenic determinant for the Lewis rat. Insertion of histidine and glycine at positions 77 and 78 in bovine...
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[NMR paper] Interaction of two complementary fragments of the bovine spinal cord myelin basic pro
Interaction of two complementary fragments of the bovine spinal cord myelin basic protein with phosphatidylglycerol bilayers, studied by 2H and 31P NMR spectroscopy.
Related Articles Interaction of two complementary fragments of the bovine spinal cord myelin basic protein with phosphatidylglycerol bilayers, studied by 2H and 31P NMR spectroscopy.
Biochemistry. 1993 Sep 21;32(37):9709-13
Authors: Hayer-Hartl M, Brophy PJ, Marsh D, Watts A
The interaction of two complementary fragments of myelin basic protein from bovine spinal cord with...
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Solid-State NMR Spectroscopy of Membrane-Associated Myelin Basic Protein-Conformation
Solid-State NMR Spectroscopy of Membrane-Associated Myelin Basic Protein-Conformation and Dynamics of an Immunodominant Epitope.
Related Articles Solid-State NMR Spectroscopy of Membrane-Associated Myelin Basic Protein-Conformation and Dynamics of an Immunodominant Epitope.
Biophys J. 2010 Aug 9;99(4):1247-1255
Authors: Ahmed MA, Bamm VV, Harauz G, Ladizhansky V
Myelin basic protein (MBP) maintains the tight multilamellar compaction of the myelin sheath in the central nervous system through peripheral binding of adjacent lipid bilayers of...