Phase separation driven by interchangeable properties in the intrinsically disordered regions of protein paralogs | Communications Biology - Nature.com
Phase separation driven by interchangeable properties in the intrinsically disordered regions of protein paralogs | Communications Biology - Nature.com
Phase separation driven by interchangeable properties in the intrinsically disordered regions of protein paralogs | Communications Biology - Nature.com
[NMR paper] Structural biology of RNA-binding proteins in the context of phase separation: What NMR and EPR can bring?
Structural biology of RNA-binding proteins in the context of phase separation: What NMR and EPR can bring?
Liquid-liquid phase separation of RNA-binding proteins underlies the formation of membraneless organelles, whose composition is dynamic and whose existence may be transient. These organelles are involved in regulation of RNA processing and translation and, if they behave abnormally, in pathologies. Because disorder phenomena are essential in their formation and dynamics, established methodology is insufficient for characterizing their structure. In this review, we consider the current...
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08-10-2021 10:54 PM
Interaction hot spots for phase separation revealed by NMR studies of a CAPRIN1 condensed phase [Biophysics and Computational Biology]
Interaction hot spots for phase separation revealed by NMR studies of a CAPRIN1 condensed phase
Tae Hun Kim, Brandon J. Payliss, Michael L. Nosella, Ian T. W. Lee, Yuki Toyama, Julie D. Forman-Kay, Lewis E. Kay...
Date: 2021-06-01
The role of biomolecular condensates in regulating biological function and the importance of dynamic interactions involving intrinsically disordered protein regions (IDRs) in their assembly are increasingly appreciated. While computational and theoretical approaches have provided significant insights into IDR phase behavior, establishing the critical...
Relationship of Sequence and Phase Separation in ProteinLow-Complexity Regions
Relationship of Sequence and Phase Separation in ProteinLow-Complexity Regions
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00008/20180316/images/medium/bi-2018-00008n_0006.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00008
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/8TxFxS7r55U
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03-17-2018 12:12 PM
[NMR paper] Revealing Conformational Variants of Solution-Phase Intrinsically Disordered Tau Protein at the Single-Molecule Level
Revealing Conformational Variants of Solution-Phase Intrinsically Disordered Tau Protein at the Single-Molecule Level
Intrinsically disordered proteins, such as tau protein, adopt a variety of conformations in solution, complicating solution-phase structural studies. We employ an anti-Brownian electrokinetic (ABEL) trap to prolong measurements of single tau proteins in solution. Once trapped, we record the fluorescence anisotropy to investigate the diversity of conformations sampled by the single molecules. A distribution of anisotropy values obtained from trapped tau protein is...
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10-24-2017 05:09 PM
[NMR paper] A Method for Systematic Assessment of Intrinsically Disordered Protein Regions by NMR.
A Method for Systematic Assessment of Intrinsically Disordered Protein Regions by NMR.
Related Articles A Method for Systematic Assessment of Intrinsically Disordered Protein Regions by NMR.
Int J Mol Sci. 2015;16(7):15743-15760
Authors: Goda N, Shimizu K, Kuwahara Y, Tenno T, Noguchi T, Ikegami T, Ota M, Hiroaki H
Abstract
Intrinsically disordered proteins (IDPs) that lack stable conformations and are highly flexible have attracted the attention of biologists. Therefore, the development of a systematic method to identify...
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07-18-2015 08:46 PM
An assignment of intrinsically disordered regions of proteins based on NMR structures
An assignment of intrinsically disordered regions of proteins based on NMR structures
January 2013
Publication year: 2013
Source:Journal of Structural Biology, Volume 181, Issue 1</br>
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Intrinsically disordered proteins (IDPs) do not adopt stable three-dimensional structures in physiological conditions, yet these proteins play crucial roles in biological phenomena. In most cases, intrinsic disorder manifests itself in segments or domains of an IDP, called intrinsically disordered regions (IDRs), but fully disordered IDPs also exist. Although IDRs can be detected as...