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10.1002/pmic.201800054 http://scihub22266oqcxt.onion/10.1002/pmic.201800054 30299594!7168002!30299594     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 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       Proteomics 2018 ; 18 (21-22): e1800054 Nephropedia Template TP {{tp|p=30299594|t=2018. Order in Disorder as Observed by the "Hydrophobic Cluster Analysis" of Protein Sequences |pdf=|usr=}}{{30299594}} gab.com Text Order in Disorder as Observed by the "Hydrophobic Cluster Analysis" of Protein Sequences JO: Proteomics http://www.kidney.de/pget.php?&tw=1&pmid=30299594 #FOAvip Hydrophobic cluster analysis (HCA) is an original approach for protein sequence analysis, which provides access to the foldable repertoire of the protein universe, including yet unannotated protein segments ("dark proteome"). Foldable segments correspond to ordered regions, as well as to intrinsically disordered regions (IDRs) undergoing disorder to order transitions. In this review, how HCA can be used to give insight into this last category of foldable segments is illustrated, with examples matching known 3D structures. After reviewing the HCA principles, examples of short foldable segments are given, which often contain short linear motifs, typically matching hydrophobic clusters. These segments become ordered upon contact with partners, with secondary structure preferences generally corresponding to those observed in the 3D structures within the complexes. Such small foldable segments are sometimes larger than the segments of known 3D structures, including flanking hydrophobic clusters that may be critical for interaction specificity or regulation, as well as intervening sequences allowing fuzziness. Cases of larger conditionally disordered domains are also presented, with lower density in hydrophobic clusters than well-folded globular domains or with exposed hydrophobic patches, which are stabilized by interaction with partners. Twit Text FOAVip Order in Disorder as Observed by the "Hydrophobic Cluster Analysis" of Protein Sequences ????Proteomics http://www.kidney.de/pget.php?&tw=1&pmid=30299594 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=30299594 #FOAvip English Wikipedia <ref>{{Cite pmid|30299594}}</ref> Order in Disorder as Observed by the "Hydrophobic Cluster Analysis" of Protein Sequences #MMPMID30299594 Bitard-Feildel T; Lamiable A; Mornon JP; Callebaut I Proteomics 2018[Nov]; 18 (21-22): e1800054 PMID30299594show ga Hydrophobic cluster analysis (HCA) is an original approach for protein sequence analysis, which provides access to the foldable repertoire of the protein universe, including yet unannotated protein segments ("dark proteome"). Foldable segments correspond to ordered regions, as well as to intrinsically disordered regions (IDRs) undergoing disorder to order transitions. In this review, how HCA can be used to give insight into this last category of foldable segments is illustrated, with examples matching known 3D structures. After reviewing the HCA principles, examples of short foldable segments are given, which often contain short linear motifs, typically matching hydrophobic clusters. These segments become ordered upon contact with partners, with secondary structure preferences generally corresponding to those observed in the 3D structures within the complexes. Such small foldable segments are sometimes larger than the segments of known 3D structures, including flanking hydrophobic clusters that may be critical for interaction specificity or regulation, as well as intervening sequences allowing fuzziness. Cases of larger conditionally disordered domains are also presented, with lower density in hydrophobic clusters than well-folded globular domains or with exposed hydrophobic patches, which are stabilized by interaction with partners. |*Cluster Analysis[MESH] |Hydrophobic and Hydrophilic Interactions[MESH] |Protein Structure, Secondary[MESH]Order in Disorder as Observed by the "Hydrophobic Cluster Analysis" of(epmc).pdf DeepDyve Pubget Overpricing