Single-molecule force spectroscopy of rapidly fluctuating, marginally stable structures in the intrinsically disordered protein α -synuclein

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DOIResolve DOI: http://doi.org/10.1103/PhysRevLett.112.158103
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TypeArticle
Journal titlePhysical Review Letters
ISSN1079-7114
Volume112
Issue15
Article number158103
SubjectOptical tweezers; Proteins; Conformational transitions; Correlation analysis; Different class; Energy landscape; Force-extension curves; Intrinsically disordered proteins; Single molecule force spectroscopy; Stable structures; Molecules; alpha synuclein; DNA; article; atomic force microscopy; chemical model; chemistry; methodology; protein conformation; protein folding; protein stability; spectroscopy; thermodynamics; alpha-Synuclein; DNA; Microscopy, Atomic Force; Models, Chemical; Protein Conformation; Protein Folding; Protein Stability; Spectrum Analysis; Thermodynamics
AbstractIntrinsically disordered proteins form transient, fluctuating structures that are difficult to observe directly. We used optical tweezers to apply force to single α-synuclein molecules and measure their extension, characterizing the resulting conformational transitions. Force-extension curves revealed rapid fluctuations at low force, arising from the folding of two different classes of structure that were only marginally stable. The energy landscape for these transitions was characterized via the force-dependent kinetics derived from correlation analysis of the extension trajectories. The barriers were small, only a few kBT, but the diffusion was slow, revealing a landscape that is flat but rough. © 2014 American Physical Society.
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LanguageEnglish
AffiliationNational Research Council Canada (NRC-CNRC); National Institute for Nanotechnology (NINT-INNT)
Peer reviewedYes
NPARC number21272183
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Record identifier8d6c016c-33d5-4b48-bfe6-7f9cc67da96f
Record created2014-07-23
Record modified2016-05-09
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