Insights on the Structure of Amyloid Fibrils from Site-Directed Mutagenesis

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Abstract:

To test the hypothesis that the ability to form ordered β-rich amyloid fibers with identical structures is a generic property of proteins we present a study on the overall structures of fibers formed by apomyoglobin mutants that either stabilize or destabilize the native state or the intermediate. Our results indicate that, at least at the macroscopic level, ordered β-rich amyloid fibers have similar structures.





Keywords: Amyloid fibrils; apomyoglobin; intermediate; protein folding; site-directed mutagenesis

Document Type: Research Article

DOI: http://dx.doi.org/10.2174/092986609789839223

Publication date: December 1, 2009

More about this publication?
  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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