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10.1016/j.cis.2014.01.015 http://scihub22266oqcxt.onion/10.1016/j.cis.2014.01.015 C4028306!4028306 !24560216     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 247.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 247.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 247.2 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\24560216 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Adv+Colloid+Interface+Sci 2014 ; 207 (ä): 223-39 Nephropedia Template TP {{tp|p=24560216 |t=2014. Comparison between the behavior of different hydrophobic peptides allowing membrane anchoring of proteins |pdf=|usr=}}{{24560216 }} gab.com Text Comparison between the behavior of different hydrophobic peptides allowing membrane anchoring of proteins JO: Adv Colloid Interface Sci http://www.kidney.de/pget.php?&tw=1&pmid=24560216 #FOAvip Membrane binding of proteins such as short chain dehydrogenase reductases or tail-anchored proteins relies on their N- and/or C-terminal hydrophobic transmembrane segment. In this review, we propose guidelines to characterize such hydrophobic peptide segments using spectroscopic and biophysical measurements. The secondary structure content of the C-terminal peptides of retinol dehydrogenase 8, RGS9-1 anchor protein, lecithin retinol acyl transferase, and of the N-terminal peptide of retinol dehydrogenase 11 has been deduced by prediction tools from their primary sequence as well as by using infrared or circular dichroism analyses. Depending on the solvent and the solubilization method, significant structural differences were observed, often involving ?-helices. The helical structure of these peptides was found to be consistent with their presumed membrane binding. Langmuir monolayers have been used as membrane models to study lipid-peptide interactions. The values of maximum insertion pressure obtained for all peptides using a monolayer of 1,2-dioleoyl-sn-glycero-3-phospho-ethanolamine (DOPE) are larger than the estimated lateral pressure of membranes, thus suggesting that they bind membranes. Polarization modulation infrared reflection absorption spectroscopy has been used to determine the structure and orientation of these peptides in the absence and in the presence of a DOPE monolayer. This lipid induced an increase or a decrease in the organization of the peptide secondary structure. Further measurements are necessary using other lipids to better understand the membrane interactions of these peptides. Twit Text FOAVip Comparison between the behavior of different hydrophobic peptides allowing membrane anchoring of proteins ????Adv Colloid Interface Sci http://www.kidney.de/pget.php?&tw=1&pmid=24560216 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24560216 #FOAvip English Wikipedia <ref>{{Cite pmid|24560216 }}</ref> Comparison between the behavior of different hydrophobic peptides allowing membrane anchoring of proteins #MMPMID24560216 Lhor M ; Bernier SC ; Horchani H ; Bussières S ; Cantin L ; Desbat B ; Salesse C Adv Colloid Interface Sci 2014[May]; 207 (ä): 223-39 PMID24560216 show ga Membrane binding of proteins such as short chain dehydrogenase reductases or tail-anchored proteins relies on their N- and/or C-terminal hydrophobic transmembrane segment. In this review, we propose guidelines to characterize such hydrophobic peptide segments using spectroscopic and biophysical measurements. The secondary structure content of the C-terminal peptides of retinol dehydrogenase 8, RGS9-1 anchor protein, lecithin retinol acyl transferase, and of the N-terminal peptide of retinol dehydrogenase 11 has been deduced by prediction tools from their primary sequence as well as by using infrared or circular dichroism analyses. Depending on the solvent and the solubilization method, significant structural differences were observed, often involving ?-helices. The helical structure of these peptides was found to be consistent with their presumed membrane binding. Langmuir monolayers have been used as membrane models to study lipid-peptide interactions. The values of maximum insertion pressure obtained for all peptides using a monolayer of 1,2-dioleoyl-sn-glycero-3-phospho-ethanolamine (DOPE) are larger than the estimated lateral pressure of membranes, thus suggesting that they bind membranes. Polarization modulation infrared reflection absorption spectroscopy has been used to determine the structure and orientation of these peptides in the absence and in the presence of a DOPE monolayer. This lipid induced an increase or a decrease in the organization of the peptide secondary structure. Further measurements are necessary using other lipids to better understand the membrane interactions of these peptides. |*Models, Biological [MESH] |Animals [MESH] |Biophysical Phenomena [MESH] |Humans [MESH] |Hydrophobic and Hydrophilic Interactions [MESH] |Lipid Bilayers/chemistry/metabolism [MESH] |Membrane Proteins/*chemistry/metabolism [MESH] |Peptide Fragments/*chemistry/metabolism [MESH] |Peptides/*chemistry/metabolism [MESH] |Phospholipids/*chemistry/metabolism [MESH] |Protein Conformation [MESH] |Protein Structure, Tertiary [MESH]Comparison between the behavior of different hydrophobic peptides allo(epmc).pdf DeepDyve Pubget Overpricing