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10.1073/pnas.1423868112 http://scihub22266oqcxt.onion/10.1073/pnas.1423868112 C4403194!4403194!25825747     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Proc+Natl+Acad+Sci+U+S+A 2015 ; 112 (15): E1908-15 Nephropedia Template TP {{tp|p=25825747|t=2015. Structural basis for the geometry-driven localization of a small protein |pdf=|usr=}}{{25825747}} gab.com Text Structural basis for the geometry-driven localization of a small protein JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=25825747 #FOAvip Despite extensive studies of protein trafficking across length scales of many microns, how proteins correctly localize within the smaller length scales of bacterial cells is still poorly understood. Recently, we proposed that slight membrane curvature, defined by the surface geometry of a bacterium, can drive the localization of certain shape-sensing proteins. Here, we developed an assay to quantify membrane curvature recognition by the small bacterial protein SpoVM and used NMR to determine the structural basis of curvature recognition. NMR and molecular dynamics simulations suggested a model wherein unusually deep membrane insertion allows the protein to sense subtle acyl chain packing differences between differently curved membranes, a distinct curvature-sensing mechanism from those used by proteins that sense high membrane curvature. Twit Text FOAVip Structural basis for the geometry-driven localization of a small protein ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=25825747 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25825747 #FOAvip English Wikipedia <ref>{{Cite pmid|25825747}}</ref> Structural basis for the geometry-driven localization of a small protein #MMPMID25825747 Gill RL; Castaing JP; Hsin J; Tan IS; Wang X; Huang KC; Tian F; Ramamurthi KS Proc Natl Acad Sci U S A 2015[Apr]; 112 (15): E1908-15 PMID25825747show ga Despite extensive studies of protein trafficking across length scales of many microns, how proteins correctly localize within the smaller length scales of bacterial cells is still poorly understood. Recently, we proposed that slight membrane curvature, defined by the surface geometry of a bacterium, can drive the localization of certain shape-sensing proteins. Here, we developed an assay to quantify membrane curvature recognition by the small bacterial protein SpoVM and used NMR to determine the structural basis of curvature recognition. NMR and molecular dynamics simulations suggested a model wherein unusually deep membrane insertion allows the protein to sense subtle acyl chain packing differences between differently curved membranes, a distinct curvature-sensing mechanism from those used by proteins that sense high membrane curvature. äStructural basis for the geometry-driven localization of a small prote(epmc).pdf DeepDyve Pubget Overpricing