[NMR paper] Visualizing Conformational Ensembles of the Nucleosome by NMR
Visualizing Conformational Ensembles of the Nucleosome by NMR
The formation of chromatin not only compacts the eukaryotic genome into the nucleus but also provides a mechanism for the regulation of all DNA templated processes. Spatial and temporal modulation of the chromatin structure is critical in such regulation and involves fine-tuned functioning of the basic subunit of chromatin, the nucleosome. It has become apparent that the nucleosome is an inherently dynamic system, but characterization of these dynamics at the atomic level has remained...
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02-24-2022 01:38 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 Studies of Dynamic Biomolecular Conformational Ensembles
NMR Studies of Dynamic Biomolecular Conformational Ensembles
Publication date: Available online 28 November 2014
Source:Progress in Nuclear Magnetic Resonance Spectroscopy</br>
Author(s): Dennis A. Torchia</br>
Multidimensional heteronuclear NMR approaches can provide nearly complete sequential signal assignments of isotopically enriched biomolecules. The availability of assignments together with measurements of spin relaxation rates, residual spin interactions, J-couplings and chemical shifts provides information at atomic resolution about internal dynamics on...
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11-29-2014 04:09 PM
[NMR paper] Loss of conformational entropy in protein folding calculated using realistic ensembles and its implications for NMR-based calculations.
Loss of conformational entropy in protein folding calculated using realistic ensembles and its implications for NMR-based calculations.
Loss of conformational entropy in protein folding calculated using realistic ensembles and its implications for NMR-based calculations.
Proc Natl Acad Sci U S A. 2014 Oct 13;
Authors: Baxa MC, Haddadian EJ, Jumper JM, Freed KF, Sosnick TR
Abstract
The loss of conformational entropy is a major contribution in the thermodynamics of protein folding. However, accurate determination of the quantity...
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10-15-2014 10:58 AM
[NMR paper] Conformational Ensembles in GPCR Activation.
Conformational Ensembles in GPCR Activation.
Related Articles Conformational Ensembles in GPCR Activation.
Cell. 2013 Jan 31;152(3):385-6
Authors: Vardy E, Roth BL
Abstract
Recent advances in G-protein-coupled receptor structural biology have provided only limited insight into the active conformations of these key signaling molecules. A paper from Nygaard et*al. reveals the dynamic nature of GPCRs along the activation pathway by complementing NMR experiments with ultralong-timescale molecular dynamics simulations.
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02-05-2013 09:51 PM
PPM: a side-chain and backbone chemical shift predictor for the assessment of protein conformational ensembles
PPM: a side-chain and backbone chemical shift predictor for the assessment of protein conformational ensembles
Abstract The combination of the wide availability of protein backbone and side-chain NMR chemical shifts with advances in understanding of their relationship to protein structure makes these parameters useful for the assessment of structural-dynamic protein models. A new chemical shift predictor (PPM) is introduced, which is solely based on physicalâ??chemical contributions to the chemical shifts for both the protein backbone and methyl-bearing amino-acid side chains. To...
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09-15-2012 09:04 AM
[NMR paper] NMR characterization of partially folded and unfolded conformational ensembles of pro
NMR characterization of partially folded and unfolded conformational ensembles of proteins.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_120x27.gif Related Articles NMR characterization of partially folded and unfolded conformational ensembles of proteins.
Biopolymers. 1999;51(3):191-207
Authors: Barbar E
Studies of unfolded and partially folded proteins provide important insight into the initiation and process of protein folding. This review focuses on the...
Resolving protein conformational ensembles using 19F-NMR and cryo-EM
Linear Mode
