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000000314 0247_ $$2DOI$$a10.1016/j.jmb.2007.11.035
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000000314 084__ $$2WoS$$aBiochemistry & Molecular Biology
000000314 1001_ $$0P:(DE-HGF)0$$aKaimann, T.$$b0
000000314 245__ $$aMolecular Model of an alpha-helical Prion Protein dimer and its monomeric subunits as derived from chemical cross-linking and molecular modeling calculations
000000314 260__ $$aAmsterdam [u.a.]$$bElsevier$$c2008
000000314 300__ $$a582 - 596
000000314 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000000314 440_0 $$03552$$aJournal of Molecular Biology$$v376$$x0022-2836$$y2
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000000314 520__ $$aPrions are the agents of a series of lethal neurodegenerative diseases. They are composed largely, if not entirely, of the host-encoded prion protein (PrP), which can exist in the cellular isoform PrP(C) and the pathological isoform PrP(Sc). The conformational change of the alpha-helical PrP(C) into beta-sheet-rich PrP(Sc) is the fundamental event of prion disease. The transition of recombinant PrP from a PrP(C)-like into a PrP(Sc)-like conformation can be induced in vitro by submicellar concentrations of SDS. An alpha-helical dimer was identified that might represent either the native state of PrP(C) or the first step from the monomeric PrP(C) to highly aggregated PrP(Sc). In the present study, the molecular structure of these dimers was analyzed by introducing covalent cross-links using 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide. Inter- and intramolecular bonds between directly neighboured amino groups and carboxy groups were generated. The bonds formed in PrP dimers of recombinant PrP (90-231) were identified by tryptic digestion and subsequent mass spectrometric analysis. Intra- and intermolecular cross-links between N-terminal glycine and three acidic amino acid side chains in the globular part of PrP were identified, showing the N-terminal amino acids (90-124) are not as flexible as known from NMR analysis. When the cross-linked sites were used as structural constraint, molecular modeling calculations yielded a structural model for PrP dimer and its monomeric subunit, including the folding of amino acids 90-124 in addition to the known structure. Molecular dynamics of the structure after release of the constraint indicated an intrinsic stability of the domain of amino acids 90-124.
000000314 536__ $$0G:(DE-Juel1)FUEK409$$2G:(DE-HGF)$$aFunktion und Dysfunktion des Nervensystems$$cP33$$x0
000000314 588__ $$aDataset connected to Web of Science, Pubmed
000000314 650_2 $$2MeSH$$aAmino Acids, Acidic: chemistry
000000314 650_2 $$2MeSH$$aAnimals
000000314 650_2 $$2MeSH$$aCircular Dichroism
000000314 650_2 $$2MeSH$$aComputer Simulation
000000314 650_2 $$2MeSH$$aCricetinae
000000314 650_2 $$2MeSH$$aCross-Linking Reagents: chemistry
000000314 650_2 $$2MeSH$$aDimerization
000000314 650_2 $$2MeSH$$aMesocricetus
000000314 650_2 $$2MeSH$$aModels, Molecular
000000314 650_2 $$2MeSH$$aNuclear Magnetic Resonance, Biomolecular
000000314 650_2 $$2MeSH$$aPrions: chemistry
000000314 650_2 $$2MeSH$$aPrions: genetics
000000314 650_2 $$2MeSH$$aPrions: metabolism
000000314 650_2 $$2MeSH$$aProtein Conformation
000000314 650_2 $$2MeSH$$aProtein Isoforms: chemistry
000000314 650_2 $$2MeSH$$aProtein Isoforms: metabolism
000000314 650_2 $$2MeSH$$aProtein Structure, Secondary
000000314 650_2 $$2MeSH$$aRecombinant Proteins: chemistry
000000314 650_2 $$2MeSH$$aRecombinant Proteins: metabolism
000000314 650_2 $$2MeSH$$aSpectrometry, Mass, Electrospray Ionization
000000314 650_2 $$2MeSH$$aTandem Mass Spectrometry
000000314 650_2 $$2MeSH$$aTrypsin: pharmacology
000000314 650_7 $$00$$2NLM Chemicals$$aAmino Acids, Acidic
000000314 650_7 $$00$$2NLM Chemicals$$aCross-Linking Reagents
000000314 650_7 $$00$$2NLM Chemicals$$aPrions
000000314 650_7 $$00$$2NLM Chemicals$$aProtein Isoforms
000000314 650_7 $$00$$2NLM Chemicals$$aRecombinant Proteins
000000314 650_7 $$0EC 3.4.21.4$$2NLM Chemicals$$aTrypsin
000000314 650_7 $$2WoSType$$aJ
000000314 7001_ $$0P:(DE-HGF)0$$aMetzger, S.$$b1
000000314 7001_ $$0P:(DE-HGF)0$$aKuhlmann, K.$$b2
000000314 7001_ $$0P:(DE-HGF)0$$aBrandt, B.$$b3
000000314 7001_ $$0P:(DE-Juel1)VDB65870$$aBirkmann, E.$$b4$$uFZJ
000000314 7001_ $$0P:(DE-HGF)0$$aHöltje, H.-D.$$b5
000000314 7001_ $$0P:(DE-HGF)0$$aRiesner, D.$$b6
000000314 773__ $$0PERI:(DE-600)1355192-9$$a10.1016/j.jmb.2007.11.035$$gVol. 376, p. 582 - 596$$p582 - 596$$q376<582 - 596$$tJournal of molecular biology$$v376$$x0022-2836$$y2008
000000314 8567_ $$uhttp://dx.doi.org/10.1016/j.jmb.2007.11.035
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000000314 9141_ $$y2008
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000000314 9201_ $$0I:(DE-Juel1)VDB805$$d31.12.2008$$gINB$$kINB-2$$lMolekulare Biophysik$$x0
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