Related ArticlesStructure and Dynamics in the Nucleosome Revealed by Solid-State NMR.
Angew Chem Int Ed Engl. 2018 Jun 14;:
Authors: Shi X, Prasanna C, Nagashima T, Yamazaki T, Pervushin K, Nordenskiöld L
Abstract
Eukaryotic chromatin structure and dynamics play key roles in genomic regulation. In the current study, the secondary structure and intramolecular dynamics of human histone H4 (hH4) in the nucleosome core particle (NCP) and in a nucleosome array are determined by solid-state NMR (SSNMR). Secondary structure elements are successfully localized in the hH4 in the NCP precipitated with Mg2+. In particular, dynamics on nanosecond to microsecond and microsecond to millisecond timescales are elucidated, revealing diverse internal motions in the hH4 protein. Relatively higher flexibility is observed for residues participating in the regulation of chromatin mobility and DNA accessibility. Furthermore, our study reveals that hH4 in the nucleosome array adopts the same structure and show similar internal dynamics as that in the NCP assembly while exhibiting relatively restricted motions in several regions consisting of residues in the N-terminus, Loop 1 and the ?3 helix region.
PMID: 29905032 [PubMed - as supplied by publisher]
[NMR paper] Dynamic Structure and Orientation of Melittin Bound to Acidic Lipid Bilayers, As Revealed by Solid-State NMR and Molecular Dynamics Simulation.
Dynamic Structure and Orientation of Melittin Bound to Acidic Lipid Bilayers, As Revealed by Solid-State NMR and Molecular Dynamics Simulation.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Dynamic Structure and Orientation of Melittin Bound to Acidic Lipid Bilayers, As Revealed by Solid-State NMR and Molecular Dynamics Simulation.
J Phys Chem B. 2017 03 02;121(8):1802-1811
Authors: Norisada K, Javkhlantugs N, Mishima D, Kawamura I, Saitô H, Ueda K, Naito A
...
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05-02-2018 11:57 AM
[NMR paper] Site-Specific Studies of Nucleosome Interactions by Solid-State NMR.
Site-Specific Studies of Nucleosome Interactions by Solid-State NMR.
Related Articles Site-Specific Studies of Nucleosome Interactions by Solid-State NMR.
Angew Chem Int Ed Engl. 2018 Feb 21;:
Authors: Xiang S, le Paige UB, Horn V, Houben K, Baldus M, van Ingen H
Abstract
Chromatin function depends on a dense network of interactions between nucleosomes and wide range of proteins. A detailed description of these protein-nucleosome interactions is required to reach a full molecular understanding of chromatin function in both...
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02-23-2018 03:44 AM
MembraneInsertion of a Dinuclear Polypyridylruthenium(II)Complex Revealed by Solid-State NMR and Molecular Dynamics Simulation:Implications for Selective Antibacterial Activity
MembraneInsertion of a Dinuclear Polypyridylruthenium(II)Complex Revealed by Solid-State NMR and Molecular Dynamics Simulation:Implications for Selective Antibacterial Activity
Daniel K. Weber, Marc-Antoine Sani, Matthew T. Downton, Frances Separovic, F. Richard Keene and J. Grant Collins
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.6b09996/20161109/images/medium/ja-2016-099965_0009.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.6b09996
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA...
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11-19-2016 08:35 PM
[NMR paper] Water scaffolding in collagen: Implications on protein dynamics as revealed by solid-state NMR.
Water scaffolding in collagen: Implications on protein dynamics as revealed by solid-state NMR.
Water scaffolding in collagen: Implications on protein dynamics as revealed by solid-state NMR.
Biopolymers. 2013 Jun 19;
Authors: Aliev AE, Courtier-Murias D
Abstract
Solid-state NMR studies of collagen samples of various origin confirm that the amplitude of collagen backbone and sidechain motions increases significantly on increasing the water content. This conclusion is supported by the changes observed in three different NMR...
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06-21-2013 01:10 PM
[NMR paper] Aggregation and dynamics of oligocholate transporters in phospholipid bilayers revealed by solid-state NMR spectroscopy.
Aggregation and dynamics of oligocholate transporters in phospholipid bilayers revealed by solid-state NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Aggregation and dynamics of oligocholate transporters in phospholipid bilayers revealed by solid-state NMR spectroscopy.
Langmuir. 2012 Dec 11;28(49):17071-8
Authors: Wang T, Widanapathirana L, Zhao Y, Hong M
Abstract
Macrocycles made of cholate building blocks were previously found to...
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05-22-2013 04:43 PM
[NMR paper] Structure and orientation of bovine lactoferrampin in the mimetic bacterial membrane as revealed by solid-state NMR and molecular dynamics simulation.
Structure and orientation of bovine lactoferrampin in the mimetic bacterial membrane as revealed by solid-state NMR and molecular dynamics simulation.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif Related Articles Structure and orientation of bovine lactoferrampin in the mimetic bacterial membrane as revealed by solid-state NMR and molecular dynamics simulation.
Biophys J. 2012 Oct 17;103(8):1735-43
Authors: Tsutsumi A, Javkhlantugs N, Kira A, Umeyama M, Kawamura I, Nishimura K, Ueda K,...
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03-21-2013 02:58 PM
Dynamic structure of bombolitin II bound to lipid bilayers as revealed by solid-state NMR and molecular-dynamics simulation.
Dynamic structure of bombolitin II bound to lipid bilayers as revealed by solid-state NMR and molecular-dynamics simulation.
Dynamic structure of bombolitin II bound to lipid bilayers as revealed by solid-state NMR and molecular-dynamics simulation.
Biophys J. 2010 Nov 17;99(10):3282-9
Authors: Toraya S, Javkhlantugs N, Mishima D, Nishimura K, Ueda K, Naito A
Bombolitin II (BLT2) is one of the hemolytic heptadecapeptides originally isolated from the venom of a bumblebee. Structure and orientation of BLT2 bound to...
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03-03-2011 12:34 PM
The effects of anticalcification treatments and hydration on the molecular dynamics of bovine pericardium collagen as revealed by 13C solid-state NMR.
The effects of anticalcification treatments and hydration on the molecular dynamics of bovine pericardium collagen as revealed by 13C solid-state NMR.
The effects of anticalcification treatments and hydration on the molecular dynamics of bovine pericardium collagen as revealed by 13C solid-state NMR.
Magn Reson Chem. 2010 Sep;48(9):704-11
Authors: deAzevedo ER, Ayrosa AM, Faria GC, Cervantes HJ, Huster D, Bonagamba TJ, Pitombo RN, Rabbani SR
This article describes a solid-state NMR (SSNMR) investigation of the influence of hydration and chemical...
Structure and Dynamics in the Nucleosome Revealed by Solid-State NMR.
Linear Mode
