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, protein folding, site-directed mutagenesis, intermediate, apomyoglobin
Protein & Peptide Letters
Title: Insights on the Structure of Amyloid Fibrils from Site-Directed Mutagenesis
Volume: 16 Issue: 12
Author(s): Daniel Henrique do Amaral Correa and Carlos Henrique Inacio Ramos
Affiliation:
Keywords: Amyloid fibrils, protein folding, site-directed mutagenesis, intermediate, apomyoglobin
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.
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Cite this article as:
Correa do Amaral Daniel Henrique and Inacio Ramos Henrique Carlos, Insights on the Structure of Amyloid Fibrils from Site-Directed Mutagenesis, Protein & Peptide Letters 2009; 16 (12) . https://dx.doi.org/10.2174/092986609789839223
DOI https://dx.doi.org/10.2174/092986609789839223 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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