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10.1038/srep13631 http://scihub22266oqcxt.onion/10.1038/srep13631 C4562173!4562173!26348154     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       Sci+Rep 2015 ; 5 (ä): ä Nephropedia Template TP {{tp|p=26348154|t=2015. Structural and Thermodynamic Characteristics of Amyloidogenic Intermediates of ?-2-Microglobulin |pdf=|usr=}}{{26348154}} gab.com Text Structural and Thermodynamic Characteristics of Amyloidogenic Intermediates of -2-Microglobulin JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=26348154 #FOAvip ?-2-microglobulin (?2m) self-aggregates to form amyloid fibril in renal patients taking long-term dialysis treatment. Despite the extensive structural and mutation studies carried out so far, the molecular details on the factors that dictate amyloidogenic potential of ?2m remain elusive. Here we report molecular dynamics simulations followed by the solvation thermodynamic analyses on the wild-type ?2m and D76N, D59P, and W60C mutants at the native (N) and so-called aggregation-prone intermediate (IT) states, which are distinguished by the native cis- and non-native trans-Pro32 backbone conformations. Three major structural and thermodynamic characteristics of the IT-state relative to the N-state in ?2m protein are detected that contribute to the increased amyloidogenic potential: (i) the disruption of the edge D-strand, (ii) the increased solvent-exposed hydrophobic interface, and (iii) the increased solvation free energy (less affinity toward solvent water). Mutation effects on these three factors are shown to exhibit a good correlation with the experimentally observed distinct amyloidogenic propensity of the D76N (+), D59P (+), and W60C (?) mutants (+/? for enhanced/decreased). Our analyses thus identify the structural and thermodynamic characteristics of the amyloidogenic intermediates, which will serve to uncover molecular mechanisms and driving forces in ?2m amyloid fibril formation. Twit Text FOAVip Structural and Thermodynamic Characteristics of Amyloidogenic Intermediates of -2-Microglobulin ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=26348154 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26348154 #FOAvip English Wikipedia <ref>{{Cite pmid|26348154}}</ref> Structural and Thermodynamic Characteristics of Amyloidogenic Intermediates of ?-2-Microglobulin #MMPMID26348154 Chong SH; Hong J; Lim S; Cho S; Lee J; Ham S Sci Rep 2015[]; 5 (ä): ä PMID26348154show ga ?-2-microglobulin (?2m) self-aggregates to form amyloid fibril in renal patients taking long-term dialysis treatment. Despite the extensive structural and mutation studies carried out so far, the molecular details on the factors that dictate amyloidogenic potential of ?2m remain elusive. Here we report molecular dynamics simulations followed by the solvation thermodynamic analyses on the wild-type ?2m and D76N, D59P, and W60C mutants at the native (N) and so-called aggregation-prone intermediate (IT) states, which are distinguished by the native cis- and non-native trans-Pro32 backbone conformations. Three major structural and thermodynamic characteristics of the IT-state relative to the N-state in ?2m protein are detected that contribute to the increased amyloidogenic potential: (i) the disruption of the edge D-strand, (ii) the increased solvent-exposed hydrophobic interface, and (iii) the increased solvation free energy (less affinity toward solvent water). Mutation effects on these three factors are shown to exhibit a good correlation with the experimentally observed distinct amyloidogenic propensity of the D76N (+), D59P (+), and W60C (?) mutants (+/? for enhanced/decreased). Our analyses thus identify the structural and thermodynamic characteristics of the amyloidogenic intermediates, which will serve to uncover molecular mechanisms and driving forces in ?2m amyloid fibril formation. äStructural and Thermodynamic Characteristics of Amyloidogenic Intermed(epmc).pdf DeepDyve Pubget Overpricing