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10.1021/jacs.6b06000 http://scihub22266oqcxt.onion/10.1021/jacs.6b06000 C5089065!5089065!27642651     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Am+Chem+Soc 2016 ; 138 (42): 13882-90 Nephropedia Template TP {{tp|p=27642651|t=2016. Assembly of Peptides Derived from ?-Sheet Regions of ?-Amyloid |pdf=|usr=}}{{27642651}} gab.com Text Assembly of Peptides Derived from -Sheet Regions of -Amyloid JO: J Am Chem Soc http://www.kidney.de/pget.php?&tw=1&pmid=27642651 #FOAvip In Alzheimer?s disease, aggregation of the ?-amyloid peptide (A?) results in the formation of oligomers and fibrils that are associated with neurodegeneration. Aggregation of A? occurs through interactions between different regions of the peptide. This paper and the accompanying paper constitute a two-part investigation of two key regions of A?: the central region and the C-terminal region. These two regions promote aggregation and adopt ?-sheet structure in the fibrils, and may also do so in the oligomers. In this paper, we study the assembly of macrocyclic ?-sheet peptides that contain residues 17?23 (LVFFAED) from the central region and residues 30?36 (AIIGLMV) from the C-terminal region. These peptides assemble to form tetramers. Each tetramer consists of two hydrogen-bonded dimers that pack through hydrophobic interactions in a sandwich-like fashion. Incorporation of a single 15N isotopic label into each peptide provides a spectroscopic probe with which to elucidate the ?-sheet assembly and interaction: 1H,15N HSQC studies facilitate the identification of the monomers and tetramers; 15N-edited NOESY studies corroborate the pairing of the dimers within the tetramers. In the following paper, J. Am. Chem. Soc.2016, DOI: 10.1021/jacs.6b06001, we will extend these studies to elucidate the coassembly of the peptides to form heterotetramers. Twit Text FOAVip Assembly of Peptides Derived from -Sheet Regions of -Amyloid ????J Am Chem Soc http://www.kidney.de/pget.php?&tw=1&pmid=27642651 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27642651 #FOAvip English Wikipedia <ref>{{Cite pmid|27642651}}</ref> Assembly of Peptides Derived from ?-Sheet Regions of ?-Amyloid #MMPMID27642651 Truex N; Wang Y; Nowick JS J Am Chem Soc 2016[Oct]; 138 (42): 13882-90 PMID27642651show ga In Alzheimer?s disease, aggregation of the ?-amyloid peptide (A?) results in the formation of oligomers and fibrils that are associated with neurodegeneration. Aggregation of A? occurs through interactions between different regions of the peptide. This paper and the accompanying paper constitute a two-part investigation of two key regions of A?: the central region and the C-terminal region. These two regions promote aggregation and adopt ?-sheet structure in the fibrils, and may also do so in the oligomers. In this paper, we study the assembly of macrocyclic ?-sheet peptides that contain residues 17?23 (LVFFAED) from the central region and residues 30?36 (AIIGLMV) from the C-terminal region. These peptides assemble to form tetramers. Each tetramer consists of two hydrogen-bonded dimers that pack through hydrophobic interactions in a sandwich-like fashion. Incorporation of a single 15N isotopic label into each peptide provides a spectroscopic probe with which to elucidate the ?-sheet assembly and interaction: 1H,15N HSQC studies facilitate the identification of the monomers and tetramers; 15N-edited NOESY studies corroborate the pairing of the dimers within the tetramers. In the following paper, J. Am. Chem. Soc.2016, DOI: 10.1021/jacs.6b06001, we will extend these studies to elucidate the coassembly of the peptides to form heterotetramers. äAssembly of Peptides Derived from ?-Sheet Regions of ?-Amyloid (epmc).pdf DeepDyve Pubget Overpricing