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10.1074/jbc.M116.770271 http://scihub22266oqcxt.onion/10.1074/jbc.M116.770271 C5418037!5418037 !28283568     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28283568 &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 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\28283568 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       J+Biol+Chem 2017 ; 292 (18 ): 7348-7357 Nephropedia Template TP {{tp|p=28283568 |t=2017. Nanostructure and stability of calcitonin amyloids |pdf=|usr=}}{{28283568 }} gab.com Text Nanostructure and stability of calcitonin amyloids JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=28283568 #FOAvip Calcitonin is a 32-amino acid thyroid hormone that can form amyloid fibrils. The structural basis of the fibril formation and stabilization is still debated and poorly understood. The reason is that NMR data strongly suggest antiparallel ?-sheet calcitonin assembly, whereas modeling studies on the short DFNKF peptide (corresponding to the sequence from Asp(15) to Phe(19) of human calcitonin and reported as the minimal amyloidogenic module) show that it assembles with parallel ?-sheets. In this work, we first predict the structure of human calcitonin through two complementary molecular dynamics (MD) methods, finding that human calcitonin forms an ?-helix. We use extensive MD simulations to compare previously proposed calcitonin fibril structures. We find that two conformations, the parallel arrangement and one of the possible antiparallel structures (with Asp(15) and Phe(19) aligned), are highly stable and ordered. Nonetheless, fibrils with parallel molecules show bulky loops formed by residues 1 to 7 located on the same side, which could limit or prevent the formation of larger amyloids. We investigate fibrils formed by the DFNKF peptide by simulating different arrangements of this amyloidogenic core sequence. We show that DFNKF fibrils are highly stable when assembled in parallel ?-sheets, whereas they quickly unfold in antiparallel conformation. Our results indicate that the DFNKF peptide represents only partially the full-length calcitonin behavior. Contrary to the full-length polypeptide, in fact, the DFNKF sequence is not stable in antiparallel conformation, suggesting that the residue flanking the amyloidogenic peptide contributes to the stabilization of the experimentally observed antiparallel ?-sheet packing. Twit Text FOAVip Nanostructure and stability of calcitonin amyloids ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=28283568 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28283568 #FOAvip English Wikipedia <ref>{{Cite pmid|28283568 }}</ref> Nanostructure and stability of calcitonin amyloids #MMPMID28283568 Rigoldi F ; Metrangolo P ; Redaelli A ; Gautieri A J Biol Chem 2017[May]; 292 (18 ): 7348-7357 PMID28283568 show ga Calcitonin is a 32-amino acid thyroid hormone that can form amyloid fibrils. The structural basis of the fibril formation and stabilization is still debated and poorly understood. The reason is that NMR data strongly suggest antiparallel ?-sheet calcitonin assembly, whereas modeling studies on the short DFNKF peptide (corresponding to the sequence from Asp(15) to Phe(19) of human calcitonin and reported as the minimal amyloidogenic module) show that it assembles with parallel ?-sheets. In this work, we first predict the structure of human calcitonin through two complementary molecular dynamics (MD) methods, finding that human calcitonin forms an ?-helix. We use extensive MD simulations to compare previously proposed calcitonin fibril structures. We find that two conformations, the parallel arrangement and one of the possible antiparallel structures (with Asp(15) and Phe(19) aligned), are highly stable and ordered. Nonetheless, fibrils with parallel molecules show bulky loops formed by residues 1 to 7 located on the same side, which could limit or prevent the formation of larger amyloids. We investigate fibrils formed by the DFNKF peptide by simulating different arrangements of this amyloidogenic core sequence. We show that DFNKF fibrils are highly stable when assembled in parallel ?-sheets, whereas they quickly unfold in antiparallel conformation. Our results indicate that the DFNKF peptide represents only partially the full-length calcitonin behavior. Contrary to the full-length polypeptide, in fact, the DFNKF sequence is not stable in antiparallel conformation, suggesting that the residue flanking the amyloidogenic peptide contributes to the stabilization of the experimentally observed antiparallel ?-sheet packing. |*Molecular Dynamics Simulation [MESH] |Amyloid/*chemistry [MESH] |Calcitonin/*chemistry [MESH] |Humans [MESH] |Peptides/*chemistry [MESH] |Protein Stability [MESH] |Protein Structure, Quaternary [MESH]Nanostructure and stability of calcitonin amyloids (epmc).pdf DeepDyve Pubget Overpricing