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10.1016/j.bpc.2015.06.011 http://scihub22266oqcxt.onion/10.1016/j.bpc.2015.06.011 C4554884!4554884 !26164502     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 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 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\26164502 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Biophys+Chem 2015 ; 206 (ä): 22-39 Nephropedia Template TP {{tp|p=26164502 |t=2015. Lipid insertion domain unfolding regulates protein orientational transition behavior in a lipid bilayer |pdf=|usr=}}{{26164502 }} gab.com Text Lipid insertion domain unfolding regulates protein orientational transition behavior in a lipid bilayer JO: Biophys Chem http://www.kidney.de/pget.php?&tw=1&pmid=26164502 #FOAvip We have used coarse-grained (CG) and united atom (UA) molecular dynamics simulations to explore the mechanisms of protein orientational transition of a model peptide (A?42) in a phosphatidylcholine/cholesterol (PC/CHO) lipid bilayer. We started with an inserted state of A?42 containing a folded (I) or unfolded (II) K28-A42 lipid insertion domain (LID), which was stabilized by the K28-snorkeling and A42-anchoring to the PC polar groups in the lipid bilayer. After a UA-to-CG transformation and a 1000ns-CG simulation for enhancing the sampling of protein orientations, we discovered two transitions: I-to-"deep inserted" state with disrupted K28-snorkeling and II-to-"deep surface" state with disrupted A42-anchoring. The new states remained stable after a CG-to-UA transformation and a 200ns-UA simulation relaxation. Significant changes in the cholesterol-binding domain of A?42 and protein-induced membrane disruptions were evident after the transitions. We propose that the conformation of the LID regulates protein orientational transitions in the lipid membrane. Twit Text FOAVip Lipid insertion domain unfolding regulates protein orientational transition behavior in a lipid bilayer ????Biophys Chem http://www.kidney.de/pget.php?&tw=1&pmid=26164502 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26164502 #FOAvip English Wikipedia <ref>{{Cite pmid|26164502 }}</ref> Lipid insertion domain unfolding regulates protein orientational transition behavior in a lipid bilayer #MMPMID26164502 Cheng KH ; Qiu L ; Cheng SY ; Vaughn MW Biophys Chem 2015[Nov]; 206 (ä): 22-39 PMID26164502 show ga We have used coarse-grained (CG) and united atom (UA) molecular dynamics simulations to explore the mechanisms of protein orientational transition of a model peptide (A?42) in a phosphatidylcholine/cholesterol (PC/CHO) lipid bilayer. We started with an inserted state of A?42 containing a folded (I) or unfolded (II) K28-A42 lipid insertion domain (LID), which was stabilized by the K28-snorkeling and A42-anchoring to the PC polar groups in the lipid bilayer. After a UA-to-CG transformation and a 1000ns-CG simulation for enhancing the sampling of protein orientations, we discovered two transitions: I-to-"deep inserted" state with disrupted K28-snorkeling and II-to-"deep surface" state with disrupted A42-anchoring. The new states remained stable after a CG-to-UA transformation and a 200ns-UA simulation relaxation. Significant changes in the cholesterol-binding domain of A?42 and protein-induced membrane disruptions were evident after the transitions. We propose that the conformation of the LID regulates protein orientational transitions in the lipid membrane. |*Protein Unfolding [MESH] |Amino Acid Sequence [MESH] |Amyloid beta-Peptides/*chemistry [MESH] |Cholesterol/*chemistry [MESH] |Humans [MESH] |Lipid Bilayers/*chemistry [MESH] |Molecular Dynamics Simulation [MESH] |Molecular Sequence Data [MESH] |Peptide Fragments/*chemistry [MESH] |Phosphatidylcholines/*chemistry [MESH]Lipid insertion domain unfolding regulates protein orientational trans(epmc).pdf DeepDyve Pubget Overpricing