Molecular chaperones play a key role in protein homeostasis by preventing misfolding and aggregation, assisting in proper protein folding, and sometimes even disaggregating formed aggregates. Chaperones achieve this through a range of transient weak protein-protein interactions, which are difficult to study using traditional structural and biophysical techniques. Nuclear magnetic resonance (NMR) spectroscopy, however, is well-suited for studying such dynamic states and interactions. A wide range...
[NMR paper] NMR insights into dynamic, multivalent interactions of intrinsically disordered regions: from discrete complexes to condensates
NMR insights into dynamic, multivalent interactions of intrinsically disordered regions: from discrete complexes to condensates
The spatial and temporal organization of interactions between proteins underlie the regulation of most cellular processes. The requirement for such interactions to be specific predisposes a view that protein-protein interactions are relatively static and are formed through the stable complementarity of the interacting partners. A growing body of reports indicate, however, that many interactions lead to fuzzy complexes with an ensemble of conformations in dynamic...
[NMR paper] Chaperone–client complexes: A dynamic liaison
Chaperone–client complexes: A dynamic liaison
Publication date: April 2018
Source:Journal of Magnetic Resonance, Volume 289</br>
Author(s): Sebastian Hiller, Björn M. Burmann</br>
Living cells contain molecular chaperones that are organized in intricate networks to surveil protein homeostasis by avoiding polypeptide misfolding, aggregation, and the generation of toxic species. In addition, cellular chaperones also fulfill a multitude of alternative functionalities: transport of clients towards a target location, help them fold, unfold misfolded species, resolve...
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[NMR paper] Solution NMR structure of CsgE: Structural insights into a chaperone and regulator protein important for functional amyloid formation.
Solution NMR structure of CsgE: Structural insights into a chaperone and regulator protein important for functional amyloid formation.
Related Articles Solution NMR structure of CsgE: Structural insights into a chaperone and regulator protein important for functional amyloid formation.
Proc Natl Acad Sci U S A. 2016 Jun 13;
Authors: Shu Q, Krezel AM, Cusumano ZT, Pinkner JS, Klein R, Hultgren SJ, Frieden C
Abstract
Curli, consisting primarily of major structural subunit CsgA, are functional amyloids produced on the surface of...
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06-15-2016 11:12 PM
[NMR paper] Chaperones and chaperone-substrate complexes: Dynamic playgrounds for NMR spectroscopists.
Chaperones and chaperone-substrate complexes: Dynamic playgrounds for NMR spectroscopists.
Related Articles Chaperones and chaperone-substrate complexes: Dynamic playgrounds for NMR spectroscopists.
Prog Nucl Magn Reson Spectrosc. 2015 Apr;86-87C:41-64
Authors: Burmann BM, Hiller S
Abstract
The majority of proteins depend on a well-defined three-dimensional structure to obtain their functionality. In the cellular environment, the process of protein folding is guided by molecular chaperones to avoid misfolding, aggregation, and...
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Chaperones and chaperone–substrate complexes: Dynamic playgrounds for NMR spectroscopists
Chaperones and chaperone–substrate complexes: Dynamic playgrounds for NMR spectroscopists
Publication date: April 2015
Source:Progress in Nuclear Magnetic Resonance Spectroscopy, Volumes 86–87</br>
Author(s): Björn M. Burmann , Sebastian Hiller</br>
The majority of proteins depend on a well-defined three-dimensional structure to obtain their functionality. In the cellular environment, the process of protein folding is guided by molecular chaperones to avoid misfolding, aggregation, and the generation of toxic species. To this end, living cells contain complex...