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...
[NMR paper] DEER-PREdict: Software for efficient calculation of spin-labeling EPR and NMR data from conformational ensembles.
DEER-PREdict: Software for efficient calculation of spin-labeling EPR and NMR data from conformational ensembles.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--journals.plos.org-ploscompbiol-resource-img-external-pcbi_120x30.png Related Articles DEER-PREdict: Software for efficient calculation of spin-labeling EPR and NMR data from conformational ensembles.
PLoS Comput Biol. 2021 Jan 22;17(1):e1008551
Authors: Tesei G, Martins JM, Kunze MBA, Wang Y, Crehuet R, Lindorff-Larsen K
Abstract
Owing to...
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[NMR paper] DNP-Enhanced MAS NMR: A Tool to Snapshot Conformational Ensembles of ?-Synuclein in Different States.
DNP-Enhanced MAS NMR: A Tool to Snapshot Conformational Ensembles of ?-Synuclein in Different States.
DNP-Enhanced MAS NMR: A Tool to Snapshot Conformational Ensembles of ?-Synuclein in Different States.
Biophys J. 2018 Apr 10;114(7):1614-1623
Authors: Uluca B, Viennet T, Petrovi? D, Shaykhalishahi H, Weirich F, Gönülalan A, Strodel B, Etzkorn M, Hoyer W, Heise H
Abstract
Intrinsically disordered proteins dynamically sample a wide conformational space and therefore do not adopt a stable and defined three-dimensional...
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[NMR paper] NMR Spectroscopic Studies of the Conformational Ensembles of Intrinsically Disordered Proteins.
NMR Spectroscopic Studies of the Conformational Ensembles of Intrinsically Disordered Proteins.
Related Articles NMR Spectroscopic Studies of the Conformational Ensembles of Intrinsically Disordered Proteins.
Adv Exp Med Biol. 2015;870:149-185
Authors: Kurzbach D, Kontaxis G, Coudevylle N, Konrat R
Abstract
Intrinsically disordered proteins (IDPs) are characterized by substantial conformational flexibility and thus not amenable to conventional structural biology techniques. Given their inherent structural flexibility NMR...
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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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NMR-Based Conformational Ensembles Explain pH-Gated Opening and Closing of OmpG Channel
NMR-Based Conformational Ensembles Explain pH-Gated Opening and Closing of OmpG Channel
Tiandi Zhuang, Christina Chisholm, Min Chen and Lukas K. Tamm
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja408206e/aop/images/medium/ja-2013-08206e_0011.gif
Journal of the American Chemical Society
DOI: 10.1021/ja408206e
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/UcxM_KhEqyU
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[NMR paper] NMR-based Conformational Ensembles Explain pH-Gated Opening and Closing of OmpG Channel.
NMR-based Conformational Ensembles Explain pH-Gated Opening and Closing of OmpG Channel.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles NMR-based Conformational Ensembles Explain pH-Gated Opening and Closing of OmpG Channel.
J Am Chem Soc. 2013 Sep 10;
Authors: Zhuang T, Chisholm C, Chen M, Tamm LK
Abstract
The outer membrane protein G (OmpG) is a monomeric 33 kDa 14-stranded ?-barrel membrane protein functioning as a non-specific porin for the uptake of...
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09-12-2013 11:02 PM
[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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[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...
Visualizing Conformational Ensembles of the Nucleosome by NMR
Linear Mode
