[NMR paper] NMR Reveals Specific Tracts within the Intrinsically Disordered Regions of the SARS-CoV-2 Nucleocapsid Protein Involved in RNA Encountering
NMR Reveals Specific Tracts within the Intrinsically Disordered Regions of the SARS-CoV-2 Nucleocapsid Protein Involved in RNA Encountering
The SARS-CoV-2 nucleocapsid (N) protein is crucial for the highly organized packaging and transcription of the genomic RNA. Studying atomic details of the role of its intrinsically disordered regions (IDRs) in RNA recognition is challenging due to the absence of structure and to the repetitive nature of their primary sequence. IDRs are known to act in concert with the folded domains of N and here we use NMR spectroscopy to identify the priming events...
[NMR paper] Conformational ensembles of an intrinsically disordered protein consistent with NMR, SAXS and single-molecule FRET.
Conformational ensembles of an intrinsically disordered protein consistent with NMR, SAXS and single-molecule FRET.
Related Articles Conformational ensembles of an intrinsically disordered protein consistent with NMR, SAXS and single-molecule FRET.
J Am Chem Soc. 2020 Aug 25;:
Authors: Gomes GW, Krzeminski M, Namini A, Martin EW, Mittag T, Head-Gordon T, Forman-Kay JD, Gradinaru CC
Abstract
Intrinsically disordered proteins (IDPs) have fluctuating heterogeneous conformations, which makes structural characterization challenging,...
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08-26-2020 02:46 PM
A J-modulated protonless NMR experiment characterizes the conformational ensemble of the intrinsically disordered protein WIP
A J-modulated protonless NMR experiment characterizes the conformational ensemble of the intrinsically disordered protein WIP
Abstract
Intrinsically disordered proteins (IDPs) are multi-conformational polypeptides that lack a single stable three-dimensional structure. It has become increasingly clear that the versatile IDPs play key roles in a multitude of biological processes, and, given their flexible nature, NMR is a leading method to investigate IDP behavior on the molecular level. Here we present an IDP-tailored J-modulated experiment designed to...
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11-19-2016 08:35 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
[NMR paper] Conformational Selection and Functional Dynamics of Calmodulin: A 19F NMR Study.
Conformational Selection and Functional Dynamics of Calmodulin: A 19F NMR Study.
Related Articles Conformational Selection and Functional Dynamics of Calmodulin: A 19F NMR Study.
Biochemistry. 2014 Aug 22;
Authors: Hoang J, Prosser RS
Abstract
Calcium-bound calmodulin (CaM-4Ca2+) is innately promiscuous with regard to its protein interaction network within the cell. A key facet to the interaction process involves conformational selection. In the absence of a binding peptide, CaM-4Ca2+ adopts an equilibrium between a native state...
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08-26-2014 01:25 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...
Conformational buffering underlies functional selection in intrinsically disordered protein regions - Nature.com
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