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10.1080/07391102.2017.1352539 http://scihub22266oqcxt.onion/10.1080/07391102.2017.1352539 C5902664!5902664!28714803     free     free     free Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Biomol+Struct+Dyn 2018 ; 36 (9): 2331-41 Nephropedia Template TP {{tp|p=28714803|t=2018. Comparing NMR and X-ray protein structure: Lindemann-like parameters and NMR disorder |pdf=|usr=}}{{28714803}} gab.com Text Comparing NMR and X-ray protein structure: Lindemann-like parameters and NMR disorder JO: J Biomol Struct Dyn http://www.kidney.de/pget.php?&tw=1&pmid=28714803 #FOAvip Disordered protein chains and segments are fast becoming a major pathway for our understanding of biological function, especially in more evolved species. However, the standard definition of disordered residues: the inability to constrain them in X-ray derived structures, is not easily applied to NMR derived structures. We carry out a statistical comparison between proteins whose structure was resolved using NMR and using X-ray protocols. We start by establishing a connection between these two protocols for obtaining protein structure. We find a close statistical correspondence between NMR and X-ray structures if fluctuations inherent to the NMR protocol are taken into account. Intuitively this tends to lend support to the validity of both NMR and X-ray protocols in deriving biomolecular models that correspond to in-vivo conditions. We then establish Lindemann-like parameters for NMR derived structures and examine what order/disorder cutoffs for these parameters are most consistent with X-ray data and how consistent are they. Finally, we find critical value of L = 4 for the best correspondence between X-ray and NMR derived order/disorder assignment, judged by maximizing the Matthews correlation, and a critical value L = 1.5 if a balance between false positive and false negative prediction is sought. We examine a few non-conforming cases, and examine the origin of the structure derived in X-ray. This study could help in assigning meaningful disorder from NMR experiments. Running Title: NMR X-ray comparison Twit Text FOAVip Comparing NMR and X-ray protein structure: Lindemann-like parameters and NMR disorder ????J Biomol Struct Dyn http://www.kidney.de/pget.php?&tw=1&pmid=28714803 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28714803 #FOAvip English Wikipedia <ref>{{Cite pmid|28714803}}</ref> Comparing NMR and X-ray protein structure: Lindemann-like parameters and NMR disorder #MMPMID28714803 Faraggi E; Dunker K; Sussman J; Kloczkowski A J Biomol Struct Dyn 2018[Jul]; 36 (9): 2331-41 PMID28714803show ga Disordered protein chains and segments are fast becoming a major pathway for our understanding of biological function, especially in more evolved species. However, the standard definition of disordered residues: the inability to constrain them in X-ray derived structures, is not easily applied to NMR derived structures. We carry out a statistical comparison between proteins whose structure was resolved using NMR and using X-ray protocols. We start by establishing a connection between these two protocols for obtaining protein structure. We find a close statistical correspondence between NMR and X-ray structures if fluctuations inherent to the NMR protocol are taken into account. Intuitively this tends to lend support to the validity of both NMR and X-ray protocols in deriving biomolecular models that correspond to in-vivo conditions. We then establish Lindemann-like parameters for NMR derived structures and examine what order/disorder cutoffs for these parameters are most consistent with X-ray data and how consistent are they. Finally, we find critical value of L = 4 for the best correspondence between X-ray and NMR derived order/disorder assignment, judged by maximizing the Matthews correlation, and a critical value L = 1.5 if a balance between false positive and false negative prediction is sought. We examine a few non-conforming cases, and examine the origin of the structure derived in X-ray. This study could help in assigning meaningful disorder from NMR experiments. Running Title: NMR X-ray comparison äComparing NMR and X-ray protein structure: Lindemann-like parameters a(epmc).pdf DeepDyve Pubget Overpricing