Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.1021/jacs.6b09454 http://scihub22266oqcxt.onion/10.1021/jacs.6b09454 C5245162!5245162 !27768305     free     free     free Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\27768305 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       J+Am+Chem+Soc 2016 ; 138 (43 ): 14214-14217 Nephropedia Template TP {{tp|p=27768305 |t=2016. Self-Assembly of Catenanes from Lasso Peptides |pdf=|usr=}}{{27768305 }} gab.com Text Self-Assembly of Catenanes from Lasso Peptides JO: J Am Chem Soc http://www.kidney.de/pget.php?&tw=1&pmid=27768305 #FOAvip Lasso peptides exist naturally in a threaded state as [1]rotaxanes, and we reasoned that lasso peptides cleaved in their loop region could serve as building blocks for catenanes. Mutagenesis of the lasso peptide microcin J25 (MccJ25) with two cysteine residues followed by cleavage of the peptide with trypsin led to a [2]rotaxane structure that self-assembled into a [3]catenane and [4]catenanes at room temperature in aqueous solution. The [3]catenane represents the smallest ring size of a catenane composed solely of polypeptide segments. The NMR structure of the [3]catenane was determined, suggesting that burial of hydrophobic residues may be a driving force for assembly of the catenane structure. Twit Text FOAVip Self-Assembly of Catenanes from Lasso Peptides ????J Am Chem Soc http://www.kidney.de/pget.php?&tw=1&pmid=27768305 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27768305 #FOAvip English Wikipedia <ref>{{Cite pmid|27768305 }}</ref> Self-Assembly of Catenanes from Lasso Peptides #MMPMID27768305 Allen CD ; Link AJ J Am Chem Soc 2016[Nov]; 138 (43 ): 14214-14217 PMID27768305 show ga Lasso peptides exist naturally in a threaded state as [1]rotaxanes, and we reasoned that lasso peptides cleaved in their loop region could serve as building blocks for catenanes. Mutagenesis of the lasso peptide microcin J25 (MccJ25) with two cysteine residues followed by cleavage of the peptide with trypsin led to a [2]rotaxane structure that self-assembled into a [3]catenane and [4]catenanes at room temperature in aqueous solution. The [3]catenane represents the smallest ring size of a catenane composed solely of polypeptide segments. The NMR structure of the [3]catenane was determined, suggesting that burial of hydrophobic residues may be a driving force for assembly of the catenane structure. |Animals [MESH] |Catenanes/*chemistry [MESH] |Models, Molecular [MESH] |Peptides/*chemistry [MESH] |Protein Conformation [MESH]Self-Assembly of Catenanes from Lasso Peptides (epmc).pdf DeepDyve Pubget Overpricing