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Statistical analysis of protein evolution suggests a design for natural proteins in which sparse networks of coevolving amino acids (termed sectors) comprise the essence of three-dimensional structure and function. However, proteins are also subject to pressures deriving from the dynamics of the evolutionary process itself--the ability to tolerate mutation(More)
Fibrils associated with amyloid disease are molecular assemblies of key biological importance, yet how cells respond to the presence of amyloid remains unclear. Cellular responses may not only depend on the chemical composition or molecular properties of the amyloid fibrils, but their physical attributes such as length, width, or surface area may also play(More)
Supplementary figure 1 Comparison of wild-type E 2 m fibrils formed at pH 7 and pH 2.5. (a) Twisted fibrils formed at pH 7 undergo extensive lateral bundling. Scale bar, 100 nm. (b) Enlargement of a pH 7 fibril, showing features of the subunit repeat along the protofilaments (red stripes). (c) Segment of a fibril formed at pH 2.5. Scale bar for b and c, 50(More)
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