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10.1002/anie.201713158 http://scihub22266oqcxt.onion/10.1002/anie.201713158 C5947581!5947581!29465771     free     free     free Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Angew+Chem+Int+Ed+Engl 2018 ; 57 (17): 4571-5 Nephropedia Template TP {{tp|p=29465771|t=2018. Site?Specific Studies of Nucleosome Interactions by Solid?State NMR Spectroscopy |pdf=|usr=}}{{29465771}} gab.com Text Site Specific Studies of Nucleosome Interactions by Solid State NMR Spectroscopy JO: Angew Chem Int Ed Engl http://www.kidney.de/pget.php?&tw=1&pmid=29465771 #FOAvip Chromatin function depends on a dense network of interactions between nucleosomes and a 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 genetics and epigenetics. Herein, we show that the structure, dynamics, and interactions of nucleosomes can be interrogated in a residue?specific manner by using state?of?the?art solid?state NMR spectroscopy. Using sedimented nucleosomes, high?resolution spectra were obtained for both flexible histone tails and the non?mobile histone core. Through co?sedimentation of a nucleosome?binding peptide, we demonstrate that protein?binding sites on the nucleosome surface can be determined. We believe that this approach holds great promise as it is generally applicable, extendable to include the structure and dynamics of the bound proteins, and scalable to interactions of proteins with higher?order chromatin structures, including isolated and cellular chromatin. Twit Text FOAVip Site Specific Studies of Nucleosome Interactions by Solid State NMR Spectroscopy ????Angew Chem Int Ed Engl http://www.kidney.de/pget.php?&tw=1&pmid=29465771 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29465771 #FOAvip English Wikipedia <ref>{{Cite pmid|29465771}}</ref> Site?Specific Studies of Nucleosome Interactions by Solid?State NMR Spectroscopy #MMPMID29465771 Xiang S; le?Paige UB; Horn V; Houben K; Baldus M; van?Ingen H Angew Chem Int Ed Engl 2018[Apr]; 57 (17): 4571-5 PMID29465771show ga Chromatin function depends on a dense network of interactions between nucleosomes and a 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 genetics and epigenetics. Herein, we show that the structure, dynamics, and interactions of nucleosomes can be interrogated in a residue?specific manner by using state?of?the?art solid?state NMR spectroscopy. Using sedimented nucleosomes, high?resolution spectra were obtained for both flexible histone tails and the non?mobile histone core. Through co?sedimentation of a nucleosome?binding peptide, we demonstrate that protein?binding sites on the nucleosome surface can be determined. We believe that this approach holds great promise as it is generally applicable, extendable to include the structure and dynamics of the bound proteins, and scalable to interactions of proteins with higher?order chromatin structures, including isolated and cellular chromatin. äSite?Specific Studies of Nucleosome Interactions by Solid?State NMR Sp(epmc).pdf DeepDyve Pubget Overpricing