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10.14440/jbm.2016.81 http://scihub22266oqcxt.onion/10.14440/jbm.2016.81 C4789767!4789767!26985443     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Biol+Methods 2016 ; 3 (1): ä Nephropedia Template TP {{tp|p=26985443|t=2016. Application of linker technique to trap transiently interacting protein complexes for structural studies |pdf=|usr=}}{{26985443}} gab.com Text Application of linker technique to trap transiently interacting protein complexes for structural studies JO: J Biol Methods http://www.kidney.de/pget.php?&tw=1&pmid=26985443 #FOAvip Protein-protein interactions are key events controlling several biological processes. We have developed and employed a method to trap transiently interacting protein complexes for structural studies using glycine-rich linkers to fuse interacting partners, one of which is unstructured. Initial steps involve isothermal titration calorimetry to identify the minimum binding region of the unstructured protein in its interaction with its stable binding partner. This is followed by computational analysis to identify the approximate site of the interaction and to design an appropriate linker length. Subsequently, fused constructs are generated and characterized using size exclusion chromatography and dynamic light scattering experiments. The structure of the chimeric protein is then solved by crystallization, and validated both in vitro and in vivo by substituting key interacting residues of the full length, unlinked proteins with alanine. This protocol offers the opportunity to study crucial and currently unattainable transient protein interactions involved in various biological processes. Twit Text FOAVip Application of linker technique to trap transiently interacting protein complexes for structural studies ????J Biol Methods http://www.kidney.de/pget.php?&tw=1&pmid=26985443 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26985443 #FOAvip English Wikipedia <ref>{{Cite pmid|26985443}}</ref> Application of linker technique to trap transiently interacting protein complexes for structural studies #MMPMID26985443 Chichili VPR; Kumar V; Sivaraman J J Biol Methods 2016[]; 3 (1): ä PMID26985443show ga Protein-protein interactions are key events controlling several biological processes. We have developed and employed a method to trap transiently interacting protein complexes for structural studies using glycine-rich linkers to fuse interacting partners, one of which is unstructured. Initial steps involve isothermal titration calorimetry to identify the minimum binding region of the unstructured protein in its interaction with its stable binding partner. This is followed by computational analysis to identify the approximate site of the interaction and to design an appropriate linker length. Subsequently, fused constructs are generated and characterized using size exclusion chromatography and dynamic light scattering experiments. The structure of the chimeric protein is then solved by crystallization, and validated both in vitro and in vivo by substituting key interacting residues of the full length, unlinked proteins with alanine. This protocol offers the opportunity to study crucial and currently unattainable transient protein interactions involved in various biological processes. äApplication of linker technique to trap transiently interacting protei(epmc).pdf DeepDyve Pubget Overpricing