Single-molecule assays for investigating protein misfolding and aggregation

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DOIResolve DOI: http://doi.org/10.1039/c3cp44564j
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TypeArticle
Journal titlePhysical Chemistry Chemical Physics
ISSN1463-9076
Volume15
Issue21
Pages79347948; # of pages: 15
Subjectatomic force microscopy; metabolism; protein folding; protein multimerization; spectrofluorometry; Amyloid; Microscopy, Atomic Force; Protein Folding; Protein Multimerization; Proteins; Spectrometry, Fluorescence
AbstractProtein misfolding and aggregation are relevant to many fields. Recently, their investigation has experienced a revival as a central topic in the research of numerous human diseases, including Parkinson's and Alzheimer's. Much has been learned from ensemble biochemical approaches, but the inherently heterogeneous nature of the underlying processes has obscured many important details. Single-molecule techniques offer unique capabilities to study heterogeneous systems, while providing high temporal and structural resolution to characterize them. In this Perspective, we give an overview of the single-molecule assays that have been applied to protein misfolding and aggregation, which are mainly based on fluorescence and force spectroscopy. We describe some of the technical challenges involved in studying aggregation at the single-molecule level and discuss what has been learned about aggregation mechanisms from the different approaches. © 2013 the Owner Societies.
Publication date
LanguageEnglish
AffiliationNational Research Council Canada (NRC-CNRC); Security and Disruptive Technologies
Peer reviewedYes
NPARC number21271856
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Record identifierdfa77858-e409-4951-a11a-fbdc74e68e5d
Record created2014-04-24
Record modified2016-05-09
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