Global ETD Search
Search theses and dissertations gathered from participating repositories worldwide. Every result links back to the library that holds it. No account is needed.
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Showing 1 to 20 of 22 for “"Amyloid fibril"”.
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Amyloid Fibril Nucleation In Reverse Micelles
The 40-residue amyloid beta protein (Abeta) is the unstructured cleavage product of a common membrane protein that is produced in large quantities, but normally cleared from the brain before it exerts any apparent toxicity. Under some conditions, however, it undergoes a conformational change and …
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Amyloid fibril formation in Alzheimer's disease
Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Chemistry, 1993.
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Amyloid fibril structure of peptides and proteins by magic angle spinning NMR spectroscopy and dynamic nuclear polarization
Amyloid fibrils are insoluble, non-crystalline protein filaments associated with a number of diseases such as Alzheimer's and Type Il diabetes. They can have a functional role in different organisms and many proteins and peptides have been found to form amyloid fibrils in vitro. We have used magic …
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Thermodynamic Characterisation of Amyloid Fibrils
Amyloid fibril related diseases include dementia, Alzheimer’s disease and Parkinsons disease and pose an increasingly large burden to global healthcare, due to the presence of an ageing population. Despite many healthcare advances, amyloid fibril diseases remain largely untreatable, with only …
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THE ROLE OF BACTERIAL AMYLOID FIBRILS IN ESCHERICHIA COLI COMPLEMENT RESISTANCE
… to the complement system. The bacterial amyloid fibril, curli, functions in bacterial adherence and the formation of biofilm. Curli-producing parental and curli-deficient mutant E. coli was compared in its survival to human complement, using in vitro serum sensitivity assays. Results …
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Solid state nuclear magnetic resonance methodology and applications to structure determination of peptides, proteins and amyloid fibrils
… peptide fragment 105-115 of transthyretin in an amyloid fibril is investigated.
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Solid-state NMR studies of α-synuclein fibril structure
… component, α-synuclein (α- syn), adopts an amyloidogenic fibrillar form in Lewy bodies. In recent years research has slowly started to unravel clear pathological links between this fibrillar protein and PD disease progression. While great progress is being made, it has become evident that …
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The Role of Force-Sensitive Interactions in Amyloid Assembly by Fungal Adhesins
… segment of their sequence, termed the amyloid-forming region (AFR). At the core of these adhesin aggregates are parallel or anti-parallel β-sheet arrays, which can layer onto other adhesin β-sheets by sidechain–sidechain interactions to form highly stable amyloid fibrils. The Als …
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Intracellular peptide library screening to derive inhibitors of Parkinson's disease associated α-synuclein aggregation
Aggregation of α-synuclein (α-syn) into toxic fibrils is a pathogenic hallmark of Parkinson’s disease (PD). This research aimed to develop peptides capable of inhibiting α-syn aggregation using a semi-rational design combined with a multiplexed intracellular Protein-fragment Complementation Assay …
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On the Kinetics of Protein Misfolding and Aggregation
Protein (mis)folding into highly ordered, fibrillar structures, amyloid fibrils, is a hallmark of several, mainly neurodegenerative, disorders. The mechanism of this supra-molecular self-assembly reaction, as well as its relationship to protein folding are not well understood. In particular, the …
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Structure and dynamics of membrane proteins from solid-state NMR
… coordination geometry of a de novo designed amyloid fibril that catalyzes ester hydrolysis. By measuring the intermolecular contacts, we determined that peptides form parallel-in- register P-sheets and further assemble into stacked bilayers in an antiparallel orientation. The zinc binding …
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Order, disorder, and protein aggregation
… process, from early nucleation events to fibril elongation. In the first study, I present a conformational ensemble of a-synuclein, the culprit protein of Parkinson's disease, constructed using a Variational Bayesian Weighting algorithm in combination with NMR data collected by our …
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Unzipping Amyloid Fibrils: How a Novel Calcium-Binding Protein, NUCB1, Prevents the Formation of Amyloid Fibrils
… we also established novel and unique anti-amyloidogenic functional ability of sNUCB1. We show that Ca<sup>2+</sup>-free sNUCB1 can inhibit fibril formation by highly amyloidogenic human Islet Amyloid PolyPeptide (hIAPP) and Amyloid-β 42 (Aβ42) peptides, as relevant to Type-2 Diabetes and …
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Investigation Into Protein Folding and Misfolding
… structure and the second is misfolding into an amyloid fibril structure. In the first-half of this work, we investigated the folding of the BI domain of the <em>Streptococcal</em> immunoglobulin-binding domain of protein G (GB1) as our model system. Using bioinformatics approaches we …
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Studies on the physical stability of a C-terminally amidated variant of GLP-1
… species which then further elongate to form amyloid fibrils. When a peptide aggregates, it leads not only to the loss of its biological activity but it can also give rise to other critical problems, e.g. toxicity and immunogenicity, associated with the formation of intermediate oligomeric …
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An interdisciplinary approach to studying mechanistic, structural and toxic features of protein aggregates associated with neurodegenerative disorders.
… with protein aggregation have been attributed to amyloidogenic species that are present during the misfolding process. In particular, oligomeric species are, however, intrinsically difficult to study as a consequence of their low abundance and highly heterogeneous nature. The first chapter of my …
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Smart Nanomaterials from Repeat Proteins and Amyloid Fibrils
… components for protein-based materials are amyloid fibrils and tandem repeat proteins. Amyloid fibrils are exceptionally strong, tough, highly-ordered structures that self-assemble from a wide range of simple building blocks. Meanwhile, tandem repeat proteins are a class of proteins that act …
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Structural Polymorphism of Alpha-Synuclein in Conditions Resembling the Cellular Environment
… (aSyn), from its functional disordered form into amyloid fibrils with characteristic β-sheet structure, as being at the centre of PD. However, many unanswered questions remain with regards to the aSyn aggregation mechanism in neurons and, in particular, the earliest steps of this process, when the …
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COMPUTATIONAL MODELLING OF PROTEIN FIBRILLATION WITH APPLICATION TO GLUCAGON
… method to model the steric zipper of amyloid fibrils (FibPreditor) is developed. The method generates an ensemble of structures for the steric zipper by a number of geometric operations and presents the most energetically favorable candidates as models of steric zipper. The method is …
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Self-assembly of a gonadotropin-releasing hormone antagonist-Teverelix
… under other conditions it was known to form fibrillar structures. The mechanism of formation of either state, and the factors affecting the stability and rate of formation of these states was largely unknown. Since the behaviour of Tv at low and high concentrations is significantly different, …
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