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Single-molecule spectroscopy of unfolded proteins and chaperonin action


Hofmann, Hagen (2014). Single-molecule spectroscopy of unfolded proteins and chaperonin action. Biological Chemistry, 395(7-8):689-698.

Abstract

In the past decade, single-molecule fluorescence techniques provided important insights into the structure and dynamics of proteins. In particular, our understanding of the heterogeneous conformational ensembles of unfolded and intrinsically disordered proteins (IDPs) improved substantially by a combination of FRET-based single-molecule techniques with concepts from polymer physics. A complete knowledge of the forces that act in unfolded polypeptide chains will not only be important to understand the initial steps of protein folding reactions, but it will also be crucial to rationalize the coupling between ligand-binding and folding of IDPs, and the interaction of denatured proteins with molecular chaperones in the crowded cellular environment. Here, I give a personalized review of some of the key findings from my own research that contributed to a more quantitative understanding of unfolded proteins and their interactions with molecular chaperones

Abstract

In the past decade, single-molecule fluorescence techniques provided important insights into the structure and dynamics of proteins. In particular, our understanding of the heterogeneous conformational ensembles of unfolded and intrinsically disordered proteins (IDPs) improved substantially by a combination of FRET-based single-molecule techniques with concepts from polymer physics. A complete knowledge of the forces that act in unfolded polypeptide chains will not only be important to understand the initial steps of protein folding reactions, but it will also be crucial to rationalize the coupling between ligand-binding and folding of IDPs, and the interaction of denatured proteins with molecular chaperones in the crowded cellular environment. Here, I give a personalized review of some of the key findings from my own research that contributed to a more quantitative understanding of unfolded proteins and their interactions with molecular chaperones

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Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:National licences > 142-005
Dewey Decimal Classification:540 Chemistry
Language:English
Date:1 January 2014
Deposited On:26 Oct 2018 15:54
Last Modified:07 Apr 2020 07:11
Publisher:De Gruyter
ISSN:1431-6730
OA Status:Green
Publisher DOI:https://doi.org/10.1515/hsz-2014-0132
Related URLs:https://www.swissbib.ch/Search/Results?lookfor=nationallicencegruyter101515hsz20140132 (Library Catalogue)
PubMed ID:24620016

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