Formation of amyloid fibrils from fully reduced hen egg white lysozyme
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چکیده
منابع مشابه
Formation and dissolution of hen egg white lysozyme amyloid fibrils in protic i..... (DOI_ 10.1039_b817590j)
Given the common knowledge that concentrated saline environments are hostile to life because of biomolecule instability, ionic liquids (ILs) (in the sense of ambient temperature liquids consisting entirely of ions) would seem one of the least likely environments for successful studies of biomolecule behavior. Yet ionic liquids are finding increasing application in the biochemical field. Reports...
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Background & Aims: Alzheimer's disease is a neurodegenerative disorder characterized by the abnormal aggregation of amyloid-β plaques in the brain. Although several studies have been done for finding effective medicines in the treatment of this disease, a drug that inhibits amyloid β aggregation and ameliorates the disorder has not been approved so far. One important therapeutic approach is use...
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Proton tautomerism is a general phenomenon in organic molecules and plays a vital role in many fields of chemistry and biochemistry. The tautomerism of salicylideneanilines [eq(1)] has attracted a considerable attention because it is closely related to thermoand photochromism. Salicylideneanilines greatly favor the enol form over the cis-keto form in the gas phase. We demonstrate here that the ...
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Introduction: Diagnosing and treating diseases associated with amyloid fibers remain a great challenge despite of intensive research carried out. One important approach in the development of therapeutics is the use of herbal extracts which are rich in aromatic small molecules. Cinnamomum verum extract (CE) contains proanthocyanidin and cinnamaldehyde, which have been suggested to be capab...
متن کاملAnalysis of Core Region from Egg White Lysozyme Forming Amyloid Fibrils
Some of the lysozyme mutants in humans cause systemic amyloidosis. Hen egg white lysozyme (HEWL) has been well studied as a model protein of amyloid fibrils formation. We previously identified an amyloid core region consisting of nine amino acids (designated as the K peptide), which is present at 54-62 in HEWL. The K peptide, with tryptophan at its C- terminus, has the ability of self-aggregati...
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ژورنال
عنوان ژورنال: Protein Science
سال: 2004
ISSN: 0961-8368,1469-896X
DOI: 10.1110/ps.03183404