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10.1016/j.ab.2014.08.024 http://scihub22266oqcxt.onion/10.1016/j.ab.2014.08.024 C4252242!4252242!25175010     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Anal+Biochem 2014 ; ä (ä): 76-82 Nephropedia Template TP {{tp|p=25175010|t=2014. Review of Methods to Assign the NMR Peaks of Reductively Methylated Proteins |pdf=|usr=}}{{25175010}} gab.com Text Review of Methods to Assign the NMR Peaks of Reductively Methylated Proteins JO: Anal Biochem http://www.kidney.de/pget.php?&tw=1&pmid=25175010 #FOAvip Reductive methylation of lysyl side-chain amines has been a successful tool in the advancement of high resolution structural biology. The utility of this method has continuously gained ground as a protein chemical modification; first, as a tool to aid protein crystallization and later, as a probe in protein nuclear magnetic resonance (NMR) spectroscopy. As an isotope-labeling strategy for NMR studies, reductive methylation has contributed to the study of protein-protein interactions and global conformational changes. While more detailed structural studies using this labeling strategy are possible, the hurdle of assigning the NMR peaks to the corresponding reductively methylated amine hinders its use. In this review, we discuss and compare strategies used to assign the NMR peaks of reductively methylated protein-amines. Twit Text FOAVip Review of Methods to Assign the NMR Peaks of Reductively Methylated Proteins ????Anal Biochem http://www.kidney.de/pget.php?&tw=1&pmid=25175010 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25175010 #FOAvip English Wikipedia <ref>{{Cite pmid|25175010}}</ref> Review of Methods to Assign the NMR Peaks of Reductively Methylated Proteins #MMPMID25175010 Roberson KJ; Macnaughtan MA Anal Biochem 2014[Dec]; ä (ä): 76-82 PMID25175010show ga Reductive methylation of lysyl side-chain amines has been a successful tool in the advancement of high resolution structural biology. The utility of this method has continuously gained ground as a protein chemical modification; first, as a tool to aid protein crystallization and later, as a probe in protein nuclear magnetic resonance (NMR) spectroscopy. As an isotope-labeling strategy for NMR studies, reductive methylation has contributed to the study of protein-protein interactions and global conformational changes. While more detailed structural studies using this labeling strategy are possible, the hurdle of assigning the NMR peaks to the corresponding reductively methylated amine hinders its use. In this review, we discuss and compare strategies used to assign the NMR peaks of reductively methylated protein-amines. äReview of Methods to Assign the NMR Peaks of Reductively Methylated Pr(epmc).pdf DeepDyve Pubget Overpricing