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10.1021/acschembio.5b00745 http://scihub22266oqcxt.onion/10.1021/acschembio.5b00745 C4795474!4795474 !26492187     free     free     free Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\26492187 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       ACS+Chem+Biol 2016 ; 11 (1 ): 61-8 Nephropedia Template TP {{tp|p=26492187 |t=2016. Construction of Lasso Peptide Fusion Proteins |pdf=|usr=}}{{26492187 }} gab.com Text Construction of Lasso Peptide Fusion Proteins JO: ACS Chem Biol http://www.kidney.de/pget.php?&tw=1&pmid=26492187 #FOAvip Lasso peptides are a family of ribosomally synthesized and post-translationally modified peptides (RiPPs) typified by an isopeptide-bonded macrocycle between the peptide N-terminus and an aspartate or glutamate side chain. The C-terminal portion of the peptide threads through the N-terminal macrocycle to give the characteristic lasso fold. Because of the inherent stability, both proteolytic and often thermal, of lasso peptides, we became interested in whether proteins could be fused to the free C-terminus of lasso peptides. Here, we demonstrate fusion of two model proteins, the artificial leucine zipper A1 and the superfolder variant of GFP, to the C-terminus of the lasso peptide astexin-1. Successful lasso cyclization of the N-terminus of these fusion proteins requires a flexible linker in between the C-terminus of the lasso peptide and the N-terminus of the protein of interest. The ability to fuse lasso peptides to a protein of interest is an important step toward phage and bacterial display systems for the high-throughput screening of lasso peptide libraries for new functions. Twit Text FOAVip Construction of Lasso Peptide Fusion Proteins ????ACS Chem Biol http://www.kidney.de/pget.php?&tw=1&pmid=26492187 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26492187 #FOAvip English Wikipedia <ref>{{Cite pmid|26492187 }}</ref> Construction of Lasso Peptide Fusion Proteins #MMPMID26492187 Zong C ; Maksimov MO ; Link AJ ACS Chem Biol 2016[Jan]; 11 (1 ): 61-8 PMID26492187 show ga Lasso peptides are a family of ribosomally synthesized and post-translationally modified peptides (RiPPs) typified by an isopeptide-bonded macrocycle between the peptide N-terminus and an aspartate or glutamate side chain. The C-terminal portion of the peptide threads through the N-terminal macrocycle to give the characteristic lasso fold. Because of the inherent stability, both proteolytic and often thermal, of lasso peptides, we became interested in whether proteins could be fused to the free C-terminus of lasso peptides. Here, we demonstrate fusion of two model proteins, the artificial leucine zipper A1 and the superfolder variant of GFP, to the C-terminus of the lasso peptide astexin-1. Successful lasso cyclization of the N-terminus of these fusion proteins requires a flexible linker in between the C-terminus of the lasso peptide and the N-terminus of the protein of interest. The ability to fuse lasso peptides to a protein of interest is an important step toward phage and bacterial display systems for the high-throughput screening of lasso peptide libraries for new functions. |Amino Acid Sequence [MESH] |Peptides/chemistry/genetics/*metabolism [MESH] |Protein Processing, Post-Translational [MESH]Construction of Lasso Peptide Fusion Proteins (epmc).pdf DeepDyve Pubget Overpricing