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10.1016/j.bpj.2013.04.043 http://scihub22266oqcxt.onion/10.1016/j.bpj.2013.04.043 C3672899!3672899 !23746514     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 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 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\23746514 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Biophys+J 2013 ; 104 (11 ): 2419-28 Nephropedia Template TP {{tp|p=23746514 |t=2013. A membrane-translocating peptide penetrates into bilayers without significant bilayer perturbations |pdf=|usr=}}{{23746514 }} gab.com Text A membrane-translocating peptide penetrates into bilayers without significant bilayer perturbations JO: Biophys J http://www.kidney.de/pget.php?&tw=1&pmid=23746514 #FOAvip Using a high throughput screen, we have identified a family of 12-residue long peptides that spontaneously translocate across membranes. These peptides function by a poorly understood mechanism that is very different from that of the well-known, highly cationic cell penetrating peptides such as the tat peptide from HIV. The newly discovered translocating peptides can carry polar cargoes across synthetic bilayers and across cellular membranes quickly and spontaneously without disrupting the membrane. Here we report on the biophysical characterization of a representative translocating peptide from the selected family, TP2, as well as a negative control peptide, ONEG, from the same library. We measured the binding of the two peptides to lipid bilayers, their secondary structure propensities, their dispositions in bilayers by neutron diffraction, and the response of the bilayer to the peptides. Compared to the negative control, TP2 has a greater propensity for membrane partitioning, although it still binds only weakly, and a higher propensity for secondary structure. Perhaps most revealing, TP2 has the ability to penetrate deep into the bilayer without causing significant bilayer perturbations, a property that may help explain its ability to translocate without bilayer permeabilization. Twit Text FOAVip A membrane-translocating peptide penetrates into bilayers without significant bilayer perturbations ????Biophys J http://www.kidney.de/pget.php?&tw=1&pmid=23746514 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=23746514 #FOAvip English Wikipedia <ref>{{Cite pmid|23746514 }}</ref> A membrane-translocating peptide penetrates into bilayers without significant bilayer perturbations #MMPMID23746514 Cruz J ; Mihailescu M ; Wiedman G ; Herman K ; Searson PC ; Wimley WC ; Hristova K Biophys J 2013[Jun]; 104 (11 ): 2419-28 PMID23746514 show ga Using a high throughput screen, we have identified a family of 12-residue long peptides that spontaneously translocate across membranes. These peptides function by a poorly understood mechanism that is very different from that of the well-known, highly cationic cell penetrating peptides such as the tat peptide from HIV. The newly discovered translocating peptides can carry polar cargoes across synthetic bilayers and across cellular membranes quickly and spontaneously without disrupting the membrane. Here we report on the biophysical characterization of a representative translocating peptide from the selected family, TP2, as well as a negative control peptide, ONEG, from the same library. We measured the binding of the two peptides to lipid bilayers, their secondary structure propensities, their dispositions in bilayers by neutron diffraction, and the response of the bilayer to the peptides. Compared to the negative control, TP2 has a greater propensity for membrane partitioning, although it still binds only weakly, and a higher propensity for secondary structure. Perhaps most revealing, TP2 has the ability to penetrate deep into the bilayer without causing significant bilayer perturbations, a property that may help explain its ability to translocate without bilayer permeabilization. |Cell Membrane/*metabolism [MESH] |Lipid Bilayers/*metabolism [MESH] |Membrane Proteins/chemistry/*metabolism [MESH] |Oligopeptides/chemistry/*metabolism [MESH] |Phosphatidylcholines/metabolism [MESH] |Protein Structure, Secondary [MESH]A membrane-translocating peptide penetrates into bilayers without sign(epmc).pdf DeepDyve Pubget Overpricing