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10.1039/c5mb00170f http://scihub22266oqcxt.onion/10.1039/c5mb00170f C4470721!4470721 !25855872     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\25855872 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Mol+Biosyst 2015 ; 11 (7 ): 1850-6 Nephropedia Template TP {{tp|p=25855872 |t=2015. High-resolution structural characterization of Noxa, an intrinsically disordered protein, by microsecond molecular dynamics simulations |pdf=|usr=}}{{25855872 }} gab.com Text High-resolution structural characterization of Noxa, an intrinsically disordered protein, by microsecond molecular dynamics simulations JO: Mol Biosyst http://www.kidney.de/pget.php?&tw=1&pmid=25855872 #FOAvip High-resolution characterization of the structure and dynamics of intrinsically disordered proteins (IDPs) remains a challenging task. Consequently, a detailed understanding of the structural and functional features of IDPs remains limited, as very few full-length disordered proteins have been structurally characterized. We have performed microsecond-long molecular dynamics (MD) simulations of Noxa, the smallest member of the large Bcl-2 family of apoptosis regulating proteins, to characterize in atomic-level detail the structural features of a disordered protein. A 2.5 ?s MD simulation starting from an unfolded state of the protein revealed the formation of a central antiparallel ?-sheet structure flanked by two disordered segments at the N- and C-terminal ends. This topology is in reasonable agreement with protein disorder predictions and available experimental data. We show that this fold plays an essential role in the intracellular function and regulation of Noxa. We demonstrate that unbiased MD simulations in combination with a modern force field reveal structural and functional features of disordered proteins at atomic-level resolution. Twit Text FOAVip High-resolution structural characterization of Noxa, an intrinsically disordered protein, by microsecond molecular dynamics simulations ????Mol Biosyst http://www.kidney.de/pget.php?&tw=1&pmid=25855872 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25855872 #FOAvip English Wikipedia <ref>{{Cite pmid|25855872 }}</ref> High-resolution structural characterization of Noxa, an intrinsically disordered protein, by microsecond molecular dynamics simulations #MMPMID25855872 Espinoza-Fonseca LM ; Kelekar A Mol Biosyst 2015[Jul]; 11 (7 ): 1850-6 PMID25855872 show ga High-resolution characterization of the structure and dynamics of intrinsically disordered proteins (IDPs) remains a challenging task. Consequently, a detailed understanding of the structural and functional features of IDPs remains limited, as very few full-length disordered proteins have been structurally characterized. We have performed microsecond-long molecular dynamics (MD) simulations of Noxa, the smallest member of the large Bcl-2 family of apoptosis regulating proteins, to characterize in atomic-level detail the structural features of a disordered protein. A 2.5 ?s MD simulation starting from an unfolded state of the protein revealed the formation of a central antiparallel ?-sheet structure flanked by two disordered segments at the N- and C-terminal ends. This topology is in reasonable agreement with protein disorder predictions and available experimental data. We show that this fold plays an essential role in the intracellular function and regulation of Noxa. We demonstrate that unbiased MD simulations in combination with a modern force field reveal structural and functional features of disordered proteins at atomic-level resolution. |*Molecular Dynamics Simulation [MESH] |Humans [MESH] |Hydrogen Bonding [MESH] |Intrinsically Disordered Proteins/chemistry [MESH] |Protein Structure, Secondary [MESH] |Protein Structure, Tertiary [MESH] |Proto-Oncogene Proteins c-bcl-2/*chemistry [MESH]High-resolution structural characterization of Noxa, an intrinsically (epmc).pdf DeepDyve Pubget Overpricing