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10.1186/s12859-016-1449-z http://scihub22266oqcxt.onion/10.1186/s12859-016-1449-z C5333176!5333176!28251875     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       BMC+Bioinformatics 2017 ; 18 (Suppl 2): ä Nephropedia Template TP {{tp|p=28251875|t=2017. Comparative visualization of protein secondary structures |pdf=|usr=}}{{28251875}} gab.com Text Comparative visualization of protein secondary structures JO: BMC Bioinformatics http://www.kidney.de/pget.php?&tw=1&pmid=28251875 #FOAvip Background: Protein function is determined by many factors, namely by its constitution, spatial arrangement, and dynamic behavior. Studying these factors helps the biochemists and biologists to better understand the protein behavior and to design proteins with modified properties. One of the most common approaches to these studies is to compare the protein structure with other molecules and to reveal similarities and differences in their polypeptide chains. Results: We support the comparison process by proposing a new visualization technique that bridges the gap between traditionally used 1D and 3D representations. By introducing the information about mutual positions of protein chains into the 1D sequential representation the users are able to observe the spatial differences between the proteins without any occlusion commonly present in 3D view. Our representation is designed to serve namely for comparison of multiple proteins or a set of time steps of molecular dynamics simulation. Conclusions: The novel representation is demonstrated on two usage scenarios. The first scenario aims to compare a set of proteins from the family of cytochromes P450 where the position of the secondary structures has a significant impact on the substrate channeling. The second scenario focuses on the protein flexibility when by comparing a set of time steps our representation helps to reveal the most dynamically changing parts of the protein chain. Twit Text FOAVip Comparative visualization of protein secondary structures ????BMC Bioinformatics http://www.kidney.de/pget.php?&tw=1&pmid=28251875 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28251875 #FOAvip English Wikipedia <ref>{{Cite pmid|28251875}}</ref> Comparative visualization of protein secondary structures #MMPMID28251875 Kocincová L; Jare?ová M; By?ka J; Parulek J; Hauser H; Kozlíková B BMC Bioinformatics 2017[]; 18 (Suppl 2): ä PMID28251875show ga Background: Protein function is determined by many factors, namely by its constitution, spatial arrangement, and dynamic behavior. Studying these factors helps the biochemists and biologists to better understand the protein behavior and to design proteins with modified properties. One of the most common approaches to these studies is to compare the protein structure with other molecules and to reveal similarities and differences in their polypeptide chains. Results: We support the comparison process by proposing a new visualization technique that bridges the gap between traditionally used 1D and 3D representations. By introducing the information about mutual positions of protein chains into the 1D sequential representation the users are able to observe the spatial differences between the proteins without any occlusion commonly present in 3D view. Our representation is designed to serve namely for comparison of multiple proteins or a set of time steps of molecular dynamics simulation. Conclusions: The novel representation is demonstrated on two usage scenarios. The first scenario aims to compare a set of proteins from the family of cytochromes P450 where the position of the secondary structures has a significant impact on the substrate channeling. The second scenario focuses on the protein flexibility when by comparing a set of time steps our representation helps to reveal the most dynamically changing parts of the protein chain. äComparative visualization of protein secondary structures (epmc).pdf DeepDyve Pubget Overpricing