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Issue 4, 2014
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Shedding light on protein folding landscapes by single-molecule fluorescence

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Abstract

Single-molecule (SM) fluorescence methods have been increasingly instrumental in our current understanding of a number of key aspects of protein folding and aggregation landscapes over the past decade. With the advantage of a model free approach and the power of probing multiple subpopulations and stochastic dynamics directly in a heterogeneous structural ensemble, SM methods have emerged as a principle technique for studying complex systems such as intrinsically disordered proteins (IDPs), globular proteins in the unfolded basin and during folding, and early steps of protein aggregation in amyloidogenesis. This review highlights the application of these methods in investigating the free energy landscapes, folding properties and dynamics of individual protein molecules and their complexes, with an emphasis on inherently flexible systems such as IDPs.

Graphical abstract: Shedding light on protein folding landscapes by single-molecule fluorescence

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Article information


Submitted
28 Aug 2013
First published
16 Dec 2013

Chem. Soc. Rev., 2014,43, 1172-1188
Article type
Review Article

Shedding light on protein folding landscapes by single-molecule fluorescence

P. R. Banerjee and A. A. Deniz, Chem. Soc. Rev., 2014, 43, 1172
DOI: 10.1039/C3CS60311C

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