Related ArticlesInteraction 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 bilayers of dimyristoylphosphatidylglycerol has been studied by broad line 2H and 31P NMR. The fragments, produced by cleavage at the single tryptophan, consist of an N-terminal portion of molecular mass 12.6 kDa and a C-terminal portion of molecular mass 5.8 kDa. The phosphatidylglycerol lipid was deuterated at all three segments of the glycerol headgroup. The approximately linear dependence of the 2H quadrupole splittings and 31P chemical shift anisotropy on protein/lipid ratio in the complexes indicates that the lipids interacting with the protein fragments were in fast exchange on the NMR time scale (approximately 10(-4)-10(-5) s). The relative gradients of the dependence on protein/lipid ratio of both these parameters decrease with the size of the protein fragment and correlate reasonably well with both the net charge on the protein and the lipid binding stoichiometries in the absence of salt. The results are therefore consistent with a model in which the perturbation of the quadrupole splittings either is determined by the net surface potential or is constant for the different protein fragments. Either possibility is consistent with the reduced activity of the fragments relative to the whole protein.
[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.
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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] Characterization of the interaction between bovine pancreatic trypsin inhibitor and t
Characterization of the interaction between bovine pancreatic trypsin inhibitor and thiocyanate by NMR.
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Biophys Chem. 1998 Apr 20;71(2-3):221-34
Authors: Jolivalt C, Böckmann A, Riès-Kautt M, Ducruix A, Guittet E
The interaction between Bovine Pancreatic Trypsin Inhibitor and thiocyanate was studied using NMR spectroscopy following several experimental approaches. The chemical shift variations of the BPTI protons in the...
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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 myelin basic protein with single bilayers on a solid support: an NMR,
Interaction of myelin basic protein with single bilayers on a solid support: an NMR, DSC and polarized infrared ATR study.
Related Articles Interaction 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...
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[NMR paper] Comparative studies of the interaction of human and bovine platelet factor 4 with hep
Comparative studies of the interaction of human and bovine platelet factor 4 with heparin using histidine NMR resonances as spectroscopic probes.
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J Protein Chem. 1993 Jun;12(3):303-9
Authors: Talpas CJ, Lee L
The pKa values of His-38 and His-50 of the heparin-binding protein, bovine platelet factor 4, are 5.6 and 6.5, respectively, as determined by 1H NMR spectroscopy. The 1H NMR...
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[NMR paper] Interaction of apocytochrome c and derived polypeptide fragments with sodium dodecyl
Interaction of apocytochrome c and derived polypeptide fragments with sodium dodecyl sulfate micelles monitored by photochemically induced dynamic nuclear polarization 1H NMR and fluorescence spectroscopy.
Related Articles Interaction of apocytochrome c and derived polypeptide fragments with sodium dodecyl sulfate micelles monitored by photochemically induced dynamic nuclear polarization 1H NMR and fluorescence spectroscopy.
Biochemistry. 1991 Apr 9;30(14):3387-95
Authors: Snel MM, Kaptein R, de Kruijff B
The topology of apocytochrome c, the...
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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...