N.M.R. studies on myelin basic protein. I. 13C spectra in aqueous solutions

Chapman, Bogdan E.; Moore, Walter J.

doi:10.1071/ch9782367

Cited by 24 publications

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“…The protein presumably forms aggregates at this pH [Smith, 19801. The lowfield aromatic resonances in a similar spectrum have been previously assigned [Chapman and Moore, 1978;Mendz et al, 19831. Resonances due to His residues at 135.65 ppm ( E ) , 131.66 ppm (y), and 117.73 ppm (6) are broad, and sensitive to pH.…”

Section: Nmr Measurementssupporting

confidence: 67%

Interaction of ganglioside G_M1 and myelin basic protein studied by carbon‐13 and proton nuclear magnetic resonance spectroscopy

Ong

1984

J of Neuroscience Research

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The interaction of the myelin basic protein (MBP) and the major endogenous ganglioside GM1 in myelin of the central nervous system has been investigated using both 500-MHz 1H and 67.89 MHz 13C NMR. Titration of MBP by GM1 resulted in 13C NMR signal shifts for the I1e and His residues of MBP at a GM1/MBP mole ratio of one or less. The carbohydrate head group of GM1 was also found to be perturbed. 1H NMR results obtained in a similar manner demonstrated the perturbation of His and Phe residues. At a GM1/MBP mole ratio of 0.5, small perturbation of Trp #116 was observed, and at mole ratios of two and beyond significant involvement of Phe residues and methylated Arg #107 was found. Met #167 was more perturbed than Met #20; hence, more extensive interaction of the lipid is occurring with the C-terminus of the protein than with the N-terminus. No resonances from GM1 bound to MBP at mole ratios of up to one appeared in the spectra. However, as the GM1/MBP mole ratio was increased to eight or greater a major conformational change of MBP was detected. An upfield shift of the GM1 midchain methylene resonance was observed for the GM1/MBP complex. This observation provides strong evidence that the state of GM1 interacting with MBP is different from that of GM1 micelles. The number of saturable GM1 binding sites on MBP is estimated to be four. The data also favor a rapid exchange between bound GM1 and GM1 micelles. Interaction of MBP with the oligosaccharide derived from GM1 was found to be weaker than with GM1. Based on our data, a model for the interaction can be proposed: the first GM1 molecule is bound to the protein molecule through its head group and hydrocarbon chains, followed by the formation of a GM1/MBP complex with a concomitant conformational change of MBP as more GM1 is added.

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Section: Nmr Measurementssupporting

confidence: 67%

Interaction of ganglioside G_M1 and myelin basic protein studied by carbon‐13 and proton nuclear magnetic resonance spectroscopy

Ong

1984

J of Neuroscience Research

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“…At neutral pH myelin basic protein aggregates even at low concentrations (Chapman & Moore, 1978;. For this reason the spectra reported here have been measured at low protein concentrations and acidic pH.…”

Section: ~~~~ ~ ~~ ~~mentioning

confidence: 98%

Interactions of myelin basic protein with mixed dodecylphosphocholine/palmitoyllysophosphatidic acid micelles

Mendz¹,

Brown²,

Martenson³

1990

Biochemistry

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The interactions of myelin basic protein and peptides derived from it with detergent micelles of lysophosphatidylglycerol, lysophosphatidylserine, palmitoyllysophosphatidic acid, and sodium lauryl sulfate, and with mixed micelles of the neutral detergent dodecylphosphocholine and the negatively charged detergent palmitoyllysophosphatidic acid, were investigated by 1H NMR spectroscopy and circular dichroic spectropolarimetry. The results with single detergents suggested that there are discrete interaction sites in the protein molecule for neutral and anionic detergent micelles and that at least some of these sites are different for each type of detergent. The data on the binding of the protein and peptides to mixed detergent micelles suggested that intramolecular interactions in the intact protein and in one of the longer peptides limited the formation of helices and also that a balance between hydrophobic and ionic forces is achieved in the interactions of the peptides with the detergents. At high detergent/protein molar ratios, hydrophobic interactions appeared to be favored.

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“…The Arg2-fl-CH2 resonance is missing in the 2D spectrum; it was assigned in 1D spectrum by default, with a chemical shift in good agreement with that observed in MBP itself (Chapman & Moore, 1978…”

Section: C Assignmentsmentioning

confidence: 56%

N.m.r. studies of myelin basic protein. Conformation of a peptide that is an antigenic determinant for B-cell reactivity

Mendz¹,

Moore²

1985

Biochemical Journal

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The peptide Gly-Arg-Ala-Ser-Asp-Tyr-Lys-Ser, derived from myelin basic protein (MBP), is part of an epitope to monoclonal antibodies to human MBP. Its conformation has been studied in aqueous solution by high-resolution one- and two-dimensional 1H and 13C n.m.r. Two-dimensional correlated spectroscopy, pH titrations and one-dimensional spin-decoupling techniques were employed to assign the spectra observed from both nuclei. Amide proton temperature coefficients, coupling constants, 13C spin-lattice relaxation times and nuclear-Overhauser-effect data provide evidence that the solution conformations of the octapeptide include a type-II beta-turn with a hydrogen bond between the CO group of Arg2 and the NH group of Asp5. The results are discussed in view of a possible conformation of the antibody receptor site.

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N.M.R. studies on myelin basic protein. I. 13C spectra in aqueous solutions

Cited by 24 publications

References 0 publications

Interaction of ganglioside G_M1 and myelin basic protein studied by carbon‐13 and proton nuclear magnetic resonance spectroscopy

Interaction of ganglioside G_M1 and myelin basic protein studied by carbon‐13 and proton nuclear magnetic resonance spectroscopy

Interactions of myelin basic protein with mixed dodecylphosphocholine/palmitoyllysophosphatidic acid micelles

N.m.r. studies of myelin basic protein. Conformation of a peptide that is an antigenic determinant for B-cell reactivity

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N.M.R. studies on myelin basic protein. I. 13C spectra in aqueous solutions

Cited by 24 publications

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Interaction of ganglioside GM1 and myelin basic protein studied by carbon‐13 and proton nuclear magnetic resonance spectroscopy

Interaction of ganglioside GM1 and myelin basic protein studied by carbon‐13 and proton nuclear magnetic resonance spectroscopy

Interactions of myelin basic protein with mixed dodecylphosphocholine/palmitoyllysophosphatidic acid micelles

N.m.r. studies of myelin basic protein. Conformation of a peptide that is an antigenic determinant for B-cell reactivity

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Interaction of ganglioside G_M1 and myelin basic protein studied by carbon‐13 and proton nuclear magnetic resonance spectroscopy

Interaction of ganglioside G_M1 and myelin basic protein studied by carbon‐13 and proton nuclear magnetic resonance spectroscopy