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10.1002/anie.201706060 http://scihub22266oqcxt.onion/10.1002/anie.201706060 C5582604!5582604!28644511     free     free     free Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Angew+Chem+Int+Ed+Engl 2017 ; 56 (32): 9497-501 Nephropedia Template TP {{tp|p=28644511|t=2017. Bacteriophage Tail?Tube Assembly Studied by Proton?Detected 4D Solid?State NMR |pdf=|usr=}}{{28644511}} gab.com Text Bacteriophage Tail Tube Assembly Studied by Proton Detected 4D Solid State NMR JO: Angew Chem Int Ed Engl http://www.kidney.de/pget.php?&tw=1&pmid=28644511 #FOAvip Obtaining unambiguous resonance assignments remains a major bottleneck in solid?state NMR studies of protein structure and dynamics. Particularly for supramolecular assemblies with large subunits (>150 residues), the analysis of crowded spectral data presents a challenge, even if three?dimensional (3D) spectra are used. Here, we present a proton?detected 4D solid?state NMR assignment procedure that is tailored for large assemblies. The key to recording 4D spectra with three indirect carbon or nitrogen dimensions with their inherently large chemical shift dispersion lies in the use of sparse non?uniform sampling (as low as 2?%). As a proof of principle, we acquired 4D (H)COCANH, (H)CACONH, and (H)CBCANH spectra of the 20?kDa bacteriophage tail?tube protein gp17.1 in a total time of two and a half weeks. These spectra were sufficient to obtain complete resonance assignments in a straightforward manner without use of previous solution NMR data. Twit Text FOAVip Bacteriophage Tail Tube Assembly Studied by Proton Detected 4D Solid State NMR ????Angew Chem Int Ed Engl http://www.kidney.de/pget.php?&tw=1&pmid=28644511 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28644511 #FOAvip English Wikipedia <ref>{{Cite pmid|28644511}}</ref> Bacteriophage Tail?Tube Assembly Studied by Proton?Detected 4D Solid?State NMR #MMPMID28644511 Zinke M; Fricke P; Samson C; Hwang S; Wall JS; Lange S; Zinn?Justin S; Lange A Angew Chem Int Ed Engl 2017[Aug]; 56 (32): 9497-501 PMID28644511show ga Obtaining unambiguous resonance assignments remains a major bottleneck in solid?state NMR studies of protein structure and dynamics. Particularly for supramolecular assemblies with large subunits (>150 residues), the analysis of crowded spectral data presents a challenge, even if three?dimensional (3D) spectra are used. Here, we present a proton?detected 4D solid?state NMR assignment procedure that is tailored for large assemblies. The key to recording 4D spectra with three indirect carbon or nitrogen dimensions with their inherently large chemical shift dispersion lies in the use of sparse non?uniform sampling (as low as 2?%). As a proof of principle, we acquired 4D (H)COCANH, (H)CACONH, and (H)CBCANH spectra of the 20?kDa bacteriophage tail?tube protein gp17.1 in a total time of two and a half weeks. These spectra were sufficient to obtain complete resonance assignments in a straightforward manner without use of previous solution NMR data. äBacteriophage Tail?Tube Assembly Studied by Proton?Detected 4D Solid?S(epmc).pdf DeepDyve Pubget Overpricing