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10.1002/pro.2964 http://scihub22266oqcxt.onion/10.1002/pro.2964 C5338234!5338234!27272395     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       Protein+Sci 2016 ; 25 (9): 1628-36 Nephropedia Template TP {{tp|p=27272395|t=2016. Network representation of protein interactions?Experimental results |pdf=|usr=}}{{27272395}} gab.com Text Network representation of protein interactions Experimental results JO: Protein Sci http://www.kidney.de/pget.php?&tw=1&pmid=27272395 #FOAvip A graph theoretical analysis of nuclear magnetic resonance (NMR) data of six different protein interactions has been presented. The representation of the protein interaction data as a graph or network reveals that all of the studied interactions are based on a common functional concept. They all involve a single densely packed hub of functionally correlated residues that mediate the ligand binding events. This is found independent of the kind of protein (folded or unfolded) or ligand (protein, polymer or small molecule). Furthermore, the power of the graph analysis is demonstrated at the examples of the Calmodulin (CaM)/Calcium and the Cold Shock Protein A (CspA)/RNA interaction. The presented approach enables the precise determination of multiple binding sites for the respective ligand molecules. Twit Text FOAVip Network representation of protein interactions Experimental results ????Protein Sci http://www.kidney.de/pget.php?&tw=1&pmid=27272395 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27272395 #FOAvip English Wikipedia <ref>{{Cite pmid|27272395}}</ref> Network representation of protein interactions?Experimental results #MMPMID27272395 Kurzbach D; Flamm AG; Sára T Protein Sci 2016[Sep]; 25 (9): 1628-36 PMID27272395show ga A graph theoretical analysis of nuclear magnetic resonance (NMR) data of six different protein interactions has been presented. The representation of the protein interaction data as a graph or network reveals that all of the studied interactions are based on a common functional concept. They all involve a single densely packed hub of functionally correlated residues that mediate the ligand binding events. This is found independent of the kind of protein (folded or unfolded) or ligand (protein, polymer or small molecule). Furthermore, the power of the graph analysis is demonstrated at the examples of the Calmodulin (CaM)/Calcium and the Cold Shock Protein A (CspA)/RNA interaction. The presented approach enables the precise determination of multiple binding sites for the respective ligand molecules. äNetwork representation of protein interactions?Experimental results (epmc).pdf DeepDyve Pubget Overpricing