Titlebook: Single-Molecule Fluorescence Spectroscopy of the Folding of a Repeat Protein; Sharona Cohen Book 2016 Springer International Publishing Sw

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2190-5053 repeat protein.Comprehensive single-molecule FRET experimen.Inthis thesis single-molecule fluorescence resonance energy transfer(FRET)spectroscopy was used to study the folding of a protein that belongsto the large and important family of repeat proteins. Cohen showsthat the dynamics of the expande

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2190-5053 in repeat proteins, which is relatedto their function in binding multiple and disparate partners. Thisconcise research summary provides useful insights for studentsbeginning a PhD in this or a related area, and researchers enteringthis field. ....978-3-319-37236-5978-3-319-09558-5Series ISSN 2190-5053 Series E-ISSN 2190-5061

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Results,to diffuse through the focus of the confocal microscope. Bursts of emitting photons from donor and acceptor fluorophores were registered by two avalanche photo diodes (APDs). Signal detection was performed using photon counting instrumentation (PicoHarp, PicoQuant). A running-average of 15 photons w

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Discussion,onsidered as an individual unit that may be folded or unfolded. Using single-molecule microscopy, we tested whether a partially unfolded state exists with one or more than one helix unfolded in the folding of CTPR3. In principle, the Ising model suggests the presence of 128 (2^7) states in the foldi

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Discussion,with one or more than one helix unfolded in the folding of CTPR3. In principle, the Ising model suggests the presence of 128 (2^7) states in the folding of 7 helices in CTPR3. However, many of these species may be unpopulated.

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