Global ETD Search

11	Conformational Flexibility and Amyloid Core Characterization of Human Immunoglobulin Light Chain Domains by Multidimensional NMR Spectroscopy Pondaven, Simon Pierre 18 December 2012 (has links) No description available. Analytical Chemistry Immunoglobulin light-chain Light chain amyloidosis Protein misfolding amyloid fibril NMR spectroscopy
12	Bri2 BRICHOS domain : Eukaryotic expression and importance of strictly conserved cysteine residues Hemmingsson, Lovisa January 2017 (has links) Alzheimer’s disease (AD), the most common form of dementia is associated with fibril formation of amyloid-ß peptides (Aß). Aß, proteolytically derived from Aß precursor protein (AßPP), is the major component of amyloid plaques in AD brains. Familial British and Danish dementias (FBD and FDD) share pathological and clinical characteristics with AD, and the underlying mechanisms are associated with amyloid formation of mutant peptides released from the Bri2 protein. Bri2 interacts with AßPP and its BRICHOS domain has been shown to delay Aß40 and Aß42 fibril formation and toxicity in vitro and in vivo. This makes Bri2 BRICHOS a promising anti-amyloid chaperone and a potential treatment strategy for AD. Furthermore, Bri2 BRICHOS possesses a general chaperone activity as it suppresses non-fibrillar aggregation of destabilized citrate synthase (CS). Recent findings show that Bri2 BRICHOS produced in E.coli can form different molecular weight assemblies, ranging from monomers to dimers and poly-disperse oligomers. The oligomers inhibit CS aggregation, whereas the monomers and dimers are more efficient against Aß42 fibrillation and neurotoxicity, respectively. The work in this thesis shows that similar Bri2 BRICHOS quaternary structures are formed in eukaryotic cells as in E.coli. Larger BRICHOS oligomers were found in cell media, derived from proteolytically processed endogenous Bri2 in SH-SY5Y cells, as well as in human embryonic kidney (HEK293) cells transfected with a Bri2 BRICHOS construct. Recombinant human Bri2 BRICHOS mutants with one or none of the two strictly conserved cysteine residues were studied. All mutant monomers become proteolytically degraded during purification, but form stable oligomers. Single Cys to Ser mutants form stable disulfide-dependent dimers that differ in ability to prevent Aß42 fibrillation, the most stable mutant (C164S) being even more efficient than the wildtype Bri2 BRICHOS dimer. This result suggests that intra or intermolecular disulfide(s) and oligomerization affect Bri2 BRICHOS stability and activity towards Aß42 fibril formation. Bri2 BRICHOS Aß Chaperone Amyloid fibril formation Alzheimer disease Eukaryotic expression Cysteine residues Biochemistry and Molecular Biology Biokemi och molekylärbiologi
13	Peptide and Protein Supramolecular Assemblies Studied by Solid-State NMR Spectroscopy Qi, Zhe 07 September 2017 (has links) No description available. Chemistry Physical Chemistry Biochemistry Biophysics solid-state NMR magic-angle spinning prion amyloid fibril peptide amphiphile pi-conjugated peptide
14	Transition of intrinsically unfolded α-synuclein into the fibrillar state characterized by NMR spectroscopy / Transition of intrinsically unfolded α-synuclein into the fibrillar state characterized by NMR spectroscopy Cho, Min-Kyu 29 October 2008 (has links) No description available. 540 Chemie Mathematics and Computer Science NMR α-synuclein Amyloidfibrillen Nativ entfaltete Proteine NMR α-synuclein amyloid fibril natively unfolded protein 35.99 SP 000: Strukturchemie
15	Solid-state NMR characterization of Alzheimer-like tau amyloid fibrils / Charakterisierung Alzheimer-verwandter Tau Amyloidfibrillen mittels Festkörper-NMR Daebel, Venita 27 August 2012 (has links) No description available. 540 Chemie SXC 000 Chemistry Morbus Alzheimer Tau Amyloid Festkörper-NMR PHF Alzheimer's Disease Tau Amyloid Fibril Solid-State NMR PHF 35.25
16	Structural Studies of Biomolecules by Dynamic Nuclear Polarization Solid-State NMR Spectroscopy Conroy, Daniel William 29 August 2019 (has links) No description available. Chemistry Solid-State NMR Spectroscopy Dynamic Nuclear Polarization Dinitroxide Biradical Polarizing Agent Solid-Phase Peptide Synthesis TOAC DNA Hoogsteen Base-Pairing Nucleosome Core Particle Amyloid Fibril Prion Protein
17	Structure and Dynamics of the Y145Stop Variant of the Human Prion Protein Studied by Magic-Angle Spinning Solid State NMR Helmus, Jonathan Jaye 06 September 2011 (has links) No description available. Biochemistry Chemistry Physical Chemistry Physics Sold State NMR NMR protein NMR prion protein, amyloid fibril amyloid structure prion structrure

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