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      Amyloid fibrils from muscle myoglobin.

      Nature

      Amino Acid Sequence, Crystallography, X-Ray, Myoglobin, chemistry, ultrastructure, Protein Conformation, Protein Folding, Protein Structure, Secondary

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          Most cited references 10

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          Principles that govern the folding of protein chains.

           C ANFINSEN (1973)
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            Protein misfolding, evolution and disease.

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              Designing conditions for in vitro formation of amyloid protofilaments and fibrils.

              We have been able to convert a small alpha/beta protein, acylphosphatase, from its soluble and native form into insoluble amyloid fibrils of the type observed in a range of pathological conditions. This was achieved by allowing slow growth in a solution containing moderate concentrations of trifluoroethanol. When analyzed with electron microscopy, the protein aggregate present in the sample after long incubation times consisted of extended, unbranched filaments of 30-50 A in width that assemble subsequently into higher order structures. This fibrillar material possesses extensive beta-sheet structure as revealed by far-UV CD and IR spectroscopy. Furthermore, the fibrils exhibit Congo red birefringence, increased fluorescence with thioflavine T and cause a red-shift of the Congo red absorption spectrum. All of these characteristics are typical of amyloid fibrils. The results indicate that formation of amyloid occurs when the native fold of a protein is destabilized under conditions in which noncovalent interactions, and in particular hydrogen bonding, within the polypeptide chain remain favorable. We suggest that amyloid formation is not restricted to a small number of protein sequences but is a property common to many, if not all, natural polypeptide chains under appropriate conditions.
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                Author and article information

                Journal
                11242064
                10.1038/35065514

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