Studying the conformational landscape of intrinsically disordered and partially folded proteins is challenging and only accessible to a few solution state techniques, such as nuclear magnetic resonance (NMR), small-angle scattering techniques, and single-molecule Förster resonance energy transfer (smFRET). While each of the techniques is sensitive to different properties of the disordered chain, such as local structural propensities, overall dimension, or intermediate- and long-range contacts,...
[ASAP] Quantitative Description of Intrinsically Disordered Proteins Using Single-Molecule FRET, NMR, and SAXS
Quantitative Description of Intrinsically Disordered Proteins Using Single-Molecule FRET, NMR, and SAXS
Samuel Naudi-Fabra, Maud Tengo, Malene Ringkjbing Jensen, Martin Blackledge, and Sigrid Milles
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.1c06264/20211124/images/medium/ja1c06264_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.1c06264
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11-25-2021 02:57 PM
[NMR paper] Ensemble description of the intrinsically disordered N-terminal domain of the Nipah virus P/V protein from combined NMR and SAXS.
Ensemble description of the intrinsically disordered N-terminal domain of the Nipah virus P/V protein from combined NMR and SAXS.
Related Articles Ensemble description of the intrinsically disordered N-terminal domain of the Nipah virus P/V protein from combined NMR and SAXS.
Sci Rep. 2020 Nov 11;10(1):19574
Authors: Schiavina M, Salladini E, Murrali MG, Tria G, Felli IC, Pierattelli R, Longhi S
Abstract
Using SAXS and NMR spectroscopy, we herein provide a high-resolution description of the intrinsically disordered N-terminal...
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11-13-2020 04:07 PM
[ASAP] 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
Gregory-Neal W. Gomes, Mickae?l Krzeminski, Ashley Namini, Erik W. Martin, Tanja Mittag, Teresa Head-Gordon, Julie D. Forman-Kay, and Claudiu C. Gradinaru
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.0c02088/20200904/images/medium/ja0c02088_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.0c02088
http://feeds.feedburner.com/~r/acs/jacsat/~4/ouvFj6sHuyQ
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09-13-2020 09:18 AM
[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
[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] Analytical description of NMR relaxation highlights correlated dynamics in intrinsically disordered proteins.
Analytical description of NMR relaxation highlights correlated dynamics in intrinsically disordered proteins.
Related Articles Analytical description of NMR relaxation highlights correlated dynamics in intrinsically disordered proteins.
Angew Chem Int Ed Engl. 2017 Aug 22;:
Authors: Blackledge M, Salvi N, Abyzov A
Abstract
The dynamic fluctuations of intrinsically disordered proteins (IDPs) define their function. Although experimental nuclear magnetic resonance (NMR) relaxation reveals the motional complexity of these highly...
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08-25-2017 04:11 AM
[NMR paper] Analytical description of NMR relaxation highlights correlated dynamics in intrinsically disordered proteins
Analytical description of NMR relaxation highlights correlated dynamics in intrinsically disordered proteins
The dynamic fluctuations of intrinsically disordered proteins (IDPs) define their function. Although experimental nuclear magnetic resonance (NMR) relaxation reveals the motional complexity of these highly flexible proteins, the absence of physical models describing IDP dynamics hinders their mechanistic interpretation. Combining molecular dynamics simulation and NMR, we introduce a framework in which distinct motions are attributed to local libration, backbone dihedral angle...
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08-23-2017 03:18 AM
[NMR paper] Comprehensive structural and dynamical view of an unfolded protein from the combination of single-molecule FRET, NMR, and SAXS.
Comprehensive structural and dynamical view of an unfolded protein from the combination of single-molecule FRET, NMR, and SAXS.
Comprehensive structural and dynamical view of an unfolded protein from the combination of single-molecule FRET, NMR, and SAXS.
Proc Natl Acad Sci U S A. 2016 Aug 26;
Authors: Aznauryan M, Delgado L, Soranno A, Nettels D, Huang JR, Labhardt AM, Grzesiek S, Schuler B
Abstract
The properties of unfolded proteins are essential both for the mechanisms of protein folding and for the function of the large...
Quantitative Description of Intrinsically Disordered Proteins Using Single-Molecule FRET, NMR, and SAXS
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