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10.1002/minf.201400090 http://scihub22266oqcxt.onion/10.1002/minf.201400090 C4502991!4502991 !26213587     free     free     free Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\26213587 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Mol+Inform 2014 ; 33 (9 ): 588-596 Nephropedia Template TP {{tp|p=26213587 |t=2014. Fractal Dimensions of Macromolecular Structures |pdf=|usr=}}{{26213587 }} gab.com Text Fractal Dimensions of Macromolecular Structures JO: Mol Inform http://www.kidney.de/pget.php?&tw=1&pmid=26213587 #FOAvip Quantifying the properties of macromolecules is a prerequisite for understanding their roles in biochemical processes. One of the less-explored geometric features of macromolecules is molecular surface irregularity, or 'roughness', which can be measured in terms of fractal dimension (D). In this study, we demonstrate that surface roughness correlates with ligand binding potential. We quantified the surface roughnesses of biological macromolecules in a large-scale survey that revealed D values between 2.0 and 2.4. The results of our study imply that surface patches involved in molecular interactions, such as ligand-binding pockets and protein-protein interfaces, exhibit greater local fluctuations in their fractal dimensions than 'inert' surface areas. We expect approximately 22 % of a protein's surface outside of the crystallographically known ligand binding sites to be ligandable. These findings provide a fresh perspective on macromolecular structure and have considerable implications for drug design as well as chemical and systems biology. Twit Text FOAVip Fractal Dimensions of Macromolecular Structures ????Mol Inform http://www.kidney.de/pget.php?&tw=1&pmid=26213587 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26213587 #FOAvip English Wikipedia <ref>{{Cite pmid|26213587 }}</ref> Fractal Dimensions of Macromolecular Structures #MMPMID26213587 Todoroff N ; Kunze J ; Schreuder H ; Hessler G ; Baringhaus KH ; Schneider G Mol Inform 2014[Sep]; 33 (9 ): 588-596 PMID26213587 show ga Quantifying the properties of macromolecules is a prerequisite for understanding their roles in biochemical processes. One of the less-explored geometric features of macromolecules is molecular surface irregularity, or 'roughness', which can be measured in terms of fractal dimension (D). In this study, we demonstrate that surface roughness correlates with ligand binding potential. We quantified the surface roughnesses of biological macromolecules in a large-scale survey that revealed D values between 2.0 and 2.4. The results of our study imply that surface patches involved in molecular interactions, such as ligand-binding pockets and protein-protein interfaces, exhibit greater local fluctuations in their fractal dimensions than 'inert' surface areas. We expect approximately 22 % of a protein's surface outside of the crystallographically known ligand binding sites to be ligandable. These findings provide a fresh perspective on macromolecular structure and have considerable implications for drug design as well as chemical and systems biology. äFractal Dimensions of Macromolecular Structures (epmc).pdf DeepDyve Pubget Overpricing