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The chaperone toolbox at the single‐molecule level: From clamping to confining
Author(s) -
Avellaneda Mario J.,
Koers Eline J.,
Naqvi Mohsin M.,
Tans Sander J.
Publication year - 2017
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.3161
Subject(s) - chaperone (clinical) , toolbox , förster resonance energy transfer , protein folding , single molecule fret , computational biology , single molecule experiment , force spectroscopy , biophysics , folding (dsp implementation) , nanotechnology , chemistry , molecule , computer science , biology , physics , fluorescence , materials science , biochemistry , engineering , medicine , organic chemistry , pathology , quantum mechanics , electrical engineering , programming language
Protein folding is well known to be supervised by a dedicated class of proteins called chaperones. However, the core mode of action of these molecular machines has remained elusive due to several reasons including the promiscuous nature of the interactions between chaperones and their many clients, as well as the dynamics and heterogeneity of chaperone conformations and the folding process itself. While troublesome for traditional bulk techniques, these properties make an excellent case for the use of single‐molecule approaches. In this review, we will discuss how force spectroscopy, fluorescence microscopy, FCS, and FRET methods are starting to zoom in on this intriguing and diverse molecular toolbox that is of direct importance for protein quality control in cells, as well as numerous degenerative conditions that depend on it.