| Probing Fibril Dissolution of the Repeat Domain of a Functional Amyloid, Pmel17, on the Microscopic and Residue Level. | |
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MedLine Citation:
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PMID: 22092386 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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Pmel17 is a human amyloid involved in melanin synthesis. A fragment of Pmel17, the repeat domain (RPT) rich in glutamic acids, forms amyloid only at mildly acidic pH. Unlike pathological amyloids, these fibrils dissolve at neutral pH, supporting a reversible aggregation-disaggregation process. Here, we study RPT dissolution using atomic force microscopy and solution-state nuclear magnetic resonance spectroscopy. Our results reveal asymmetric fibril disassembly proceeding in the absence of intermediates. We suggest that fibril unfolding involves multiple deprotonation events resulting in electrostatic charge repulsion and filament dissolution. |
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Authors:
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Ryan P McGlinchey; James M Gruschus; Attila Nagy; Jennifer C Lee |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2011-11-17 |
Journal Detail:
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Title: Biochemistry Volume: - ISSN: 1520-4995 ISO Abbreviation: - Publication Date: 2011 Nov |
Date Detail:
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Created Date: 2011-11-18 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0370623 Medline TA: Biochemistry Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
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Laboratory of Molecular Biophysics and ‡Laboratory of Molecular Physiology, National Heart, Lung, and Blood Institute, National Institutes of Health , Bethesda, Maryland 20892, United States. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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