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The correlation between neurodegenerative disease and protein aggregation in the brain has long been recognized, but a causal relationship has not been unequivocally established, in part because a discrete pathogenic aggregate has not been identified. The ...
Aspects of conformational transitions, folding, and misfolding of peptides and proteins have recently taken center stage in various domains at the interface of chemistry, biology, and medicine because of their impact on protein misfolding diseases. Due to ...
Conformational transitions of peptides and proteins have recently moved to the center of interest in various domains of research at the interface of chemistry, biology, and medicine due to their implication in an increasing number of diseases in which the ...
Protein aggregation--and, more specifically, amyloid fibril formation--has been implicated as a primary cause of neurodegeneration in Alzheimer's disease, Parkinson's disease, and related disorders, but the mechanism by which this process triggers neuronal ...
Electron microscopy (EM) has played a central role in our current understanding of the mechanisms underlying the pathogenesis of several amyloid diseases, including Alzheimer's disease, Parkinson's disease, and prion diseases. In this chapter, we discuss t ...
We recently discovered that wheat gluten could be formed into a tough, plasticlike substance when thiol-terminated, star-branched molecules are incorporated directly into the protein structure. This discovery offers the exciting possibility of developing b ...
Cells are constantly subjected to stresses; these stresses take the form of heat, heavy metals, metabolic poisons, non-native peptides, and many others. All of these stresses have the potential to cause protein misfolding, which drives protein aggregation. ...
Recent EPR-measurements on the mouse prion protein (mPrP) have indicated that the structured C-terminal domain is capable of binding Cu(II) with high affinity. The structure of Cu(II) binding sites in PrPc are unravelled by exploiting mixed quantum-classic ...
A novel concept for triggering conformational transitions, and thus changes in structure and function, in peptides with a switching element S provides intriguing perspectives for studying mol. processes that play a key role, for example, in early events of ...
Anachelin, a complex secondary metabolite isolated from Anabaena cylindrica, possesses an unusual structure combining polyketide, peptide and alkaloid building blocks. This natural product was postulated to act as siderophore with catecholate and salicylat ...