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10.7554/eLife.30493 http://scihub22266oqcxt.onion/10.7554/eLife.30493 C5690283!5690283!29083305     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=29083305&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       eLife 2017 ; 6 (ä): ä Nephropedia Template TP {{tp|p=29083305|t=2017. Single-molecule force spectroscopy of protein-membrane interactions |pdf=|usr=}}{{29083305}} gab.com Text Single-molecule force spectroscopy of protein-membrane interactions JO: eLife http://www.kidney.de/pget.php?&tw=1&pmid=29083305 #FOAvip Many biological processes rely on protein?membrane interactions in the presence of mechanical forces, yet high resolution methods to quantify such interactions are lacking. Here, we describe a single-molecule force spectroscopy approach to quantify membrane binding of C2 domains in Synaptotagmin-1 (Syt1) and Extended Synaptotagmin-2 (E-Syt2). Syts and E-Syts bind the plasma membrane via multiple C2 domains, bridging the plasma membrane with synaptic vesicles or endoplasmic reticulum to regulate membrane fusion or lipid exchange, respectively. In our approach, single proteins attached to membranes supported on silica beads are pulled by optical tweezers, allowing membrane binding and unbinding transitions to be measured with unprecedented spatiotemporal resolution. C2 domains from either protein resisted unbinding forces of 2?7 pN and had binding energies of 4?14 kBT per C2 domain. Regulation by bilayer composition or Ca2+ recapitulated known properties of both proteins. The method can be widely applied to study protein?membrane interactions. Twit Text FOAVip Single-molecule force spectroscopy of protein-membrane interactions ????eLife http://www.kidney.de/pget.php?&tw=1&pmid=29083305 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29083305 #FOAvip English Wikipedia <ref>{{Cite pmid|29083305}}</ref> Single-molecule force spectroscopy of protein-membrane interactions #MMPMID29083305 Ma L; Cai Y; Li Y; Jiao J; Wu Z; O'Shaughnessy B; De Camilli P; Karatekin E; Zhang Y eLife 2017[]; 6 (ä): ä PMID29083305show ga Many biological processes rely on protein?membrane interactions in the presence of mechanical forces, yet high resolution methods to quantify such interactions are lacking. Here, we describe a single-molecule force spectroscopy approach to quantify membrane binding of C2 domains in Synaptotagmin-1 (Syt1) and Extended Synaptotagmin-2 (E-Syt2). Syts and E-Syts bind the plasma membrane via multiple C2 domains, bridging the plasma membrane with synaptic vesicles or endoplasmic reticulum to regulate membrane fusion or lipid exchange, respectively. In our approach, single proteins attached to membranes supported on silica beads are pulled by optical tweezers, allowing membrane binding and unbinding transitions to be measured with unprecedented spatiotemporal resolution. C2 domains from either protein resisted unbinding forces of 2?7 pN and had binding energies of 4?14 kBT per C2 domain. Regulation by bilayer composition or Ca2+ recapitulated known properties of both proteins. The method can be widely applied to study protein?membrane interactions. äSingle-molecule force spectroscopy of protein-membrane interactions (epmc).pdf DeepDyve Pubget Overpricing