The chaperone toolbox at the single-molecule level: From clamping to confining.

Autor: Avellaneda MJ; AMOLF institute, Science Park 104, 1098XG Amsterdam, The Netherlands., Koers EJ; AMOLF institute, Science Park 104, 1098XG Amsterdam, The Netherlands., Naqvi MM; AMOLF institute, Science Park 104, 1098XG Amsterdam, The Netherlands., Tans SJ; AMOLF institute, Science Park 104, 1098XG Amsterdam, The Netherlands.
Jazyk: angličtina
Zdroj: Protein science : a publication of the Protein Society [Protein Sci] 2017 Jul; Vol. 26 (7), pp. 1291-1302. Date of Electronic Publication: 2017 Apr 20.
DOI: 10.1002/pro.3161
Abstrakt: 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.
(© 2017 The Protein Society.)
Databáze: MEDLINE
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