Related ArticlesProton 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 MBP greatly reduces the encephalitogenicity of the protein. Synthetic peptides analogous to this region of MBP containing glycine and histidine are encephalitogenic if they lack the N-terminal half, residues 69-74. However, if they contain both histidine plus the N-terminal half, encephalitogenicity is abolished, suggesting that an interaction of histidine with an amino acid in the N-terminal half changes the conformation or the properties of the peptide. This was investigated by measuring the 1H-NMR spectra of synthetic peptides analogous to this region of MBP, both containing histidine but with and without the N-terminal half. The major difference in the spectra of the two peptides was the pH dependence of line broadening of the histidine resonances. The histidine C2H and C4H resonances were broadened at intermediate pH values in both peptides. However, sharpening of the lines at high pH showed a different pH dependence in the two peptides. For the longer peptide containing the N-terminal half, the lines did not sharpen until the pH was increased above 10.2, coinciding with the pKa of Lys-74. Acetylation of this peptide caused the pH at which the lines began to sharpen to drop to 8.8. In the shorter peptide, lacking the N-terminal half and Lys-74, the lines also sharpened at pH 8.8. The greater broadening which persisted up above pH 10 for the longer peptide suggests slow exchange between two different conformations or environments of the histidine. One of these could be a conformation in which the deprotonated histidine hydrogen bonds with Lys-74. The Lys side-chain resonances indicated a decrease in rotational freedom above the pKa of histidine, consistent with this conclusion. Although this putative interaction between His and Lys-74 did not appear to have a significant effect on the overall conformation of the peptide, it could result in a reduction in encephalitogenicity by altering the properties of the peptide. This could affect processing and presentation of this determinant by antigen presenting cells.
[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.
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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] Nucleotide binding by the nitrogenase Fe protein: a 31P NMR study of ADP and ATP inte
Nucleotide binding by the nitrogenase Fe protein: a 31P NMR study of ADP and ATP interactions with the Fe protein of Klebsiella pneumoniae.
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Biochem J. 1998 Sep 15;334 ( Pt 3):601-7
Authors: Miller RW, Eady RR, Gormal C, Fairhurst SA, Smith BE
Investigation of the interaction of MgADP- and MgATP2- with the Fe protein of Klebsiella pneumoniae nitrogenase by 31P NMR showed that the adenine...
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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.
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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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[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.
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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] Proton NMR study on a histone-like protein, HU alpha, from Escherichia coli and its c
Proton NMR study on a histone-like protein, HU alpha, from Escherichia coli and its complex with oligo DNAs.
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Biol Pharm Bull. 1993 May;16(5):437-43
Authors: Shindo H, Kurumizaka H, Furubayashi A, Sakuma C, Matsumoto U, Yanagida A, Goshima N, Kano Y, Imamoto F
It was confirmed that the flexible arm region of HU alpha forms an antiparallel beta-sheet and that all of the residues of phenylalanines, together with some of...
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[NMR paper] Metal complexes as allosteric effectors of human hemoglobin: an NMR study of the inte
Metal complexes as allosteric effectors of human hemoglobin: an NMR study of the interaction of the gadolinium(III) bis(m-boroxyphenylamide)diethylenetriaminepentaacetic acid complex with human oxygenated and deoxygenated hemoglobin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Metal complexes as allosteric effectors of human hemoglobin: an NMR study of the interaction of the...
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Solid-State NMR Spectroscopy of Membrane-Associated Myelin Basic Protein-Conformation
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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...