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10.1016/j.bbapap.2014.12.009 http://scihub22266oqcxt.onion/10.1016/j.bbapap.2014.12.009 C4302013!4302013!25542374     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       Biochim+Biophys+Acta 2015 ; 1854 (3): 218-28 Nephropedia Template TP {{tp|p=25542374|t=2015. Role of monomer arrangement in the amyloid self-assembly |pdf=|usr=}}{{25542374}} gab.com Text Role of monomer arrangement in the amyloid self-assembly JO: Biochim Biophys Acta http://www.kidney.de/pget.php?&tw=1&pmid=25542374 #FOAvip Assembly of amyloid proteins into aggregates requires the ordering of the monomers in oligomers and especially in such highly organized structures as fibrils. This ordering is accompanied by structural transitions leading to the formation of ordered ?-structural motifs in proteins and peptides lacking secondary structures. To characterize the effect of the monomers arrangements on the aggregation process at various stages, we performed comparative studies of the yeast prion protein Sup35 heptapeptide (GNNQQNY) along with its dimeric form CGNNQQNY-(d-Pro)-G-GNNQQNY. The (d-Pro)-G linker in this construct is capable of adopting a ?-turn, facilitating the assembly of the dimer into the dimeric antiparallel hairpin structure (AP-hairpin). We applied Atomic Force Microscopy (AFM) techniques to follow peptide-peptide interactions at the single molecule level, to visualize the morphology of aggregates formed by both constructs, thioflavin T (ThT) fluorescence to follow the aggregation kinetics, and circular dichroism (CD) spectroscopy to characterize the secondary structure of the constructs. The ThT fluorescence data showed that the AP-hairpin aggregation kinetics is insensitive to the external environment such as ionic strength and pH contrary to the monomers the kinetics of which depends dramatically on the ionic strength and pH. The AFM topographic imaging revealed that AP--hairpins primarily assemble into globular aggregates, whereas linear fibrils are primary assemblies of the monomers suggesting that both constructs follow different aggregation pathways during the self-assembly. These morphological differences are in line with the AFM force spectroscopy experiments and CD spectroscopy measurements, suggesting that the AP-hairpin is structurally rigid regardless of changes of environmental factors. Twit Text FOAVip Role of monomer arrangement in the amyloid self-assembly ????Biochim Biophys Acta http://www.kidney.de/pget.php?&tw=1&pmid=25542374 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25542374 #FOAvip English Wikipedia <ref>{{Cite pmid|25542374}}</ref> Role of monomer arrangement in the amyloid self-assembly #MMPMID25542374 Portillo A; Hashemi M; Zhang Y; Breydo L; Uversky VN; Lyubchenko YL Biochim Biophys Acta 2015[Mar]; 1854 (3): 218-28 PMID25542374show ga Assembly of amyloid proteins into aggregates requires the ordering of the monomers in oligomers and especially in such highly organized structures as fibrils. This ordering is accompanied by structural transitions leading to the formation of ordered ?-structural motifs in proteins and peptides lacking secondary structures. To characterize the effect of the monomers arrangements on the aggregation process at various stages, we performed comparative studies of the yeast prion protein Sup35 heptapeptide (GNNQQNY) along with its dimeric form CGNNQQNY-(d-Pro)-G-GNNQQNY. The (d-Pro)-G linker in this construct is capable of adopting a ?-turn, facilitating the assembly of the dimer into the dimeric antiparallel hairpin structure (AP-hairpin). We applied Atomic Force Microscopy (AFM) techniques to follow peptide-peptide interactions at the single molecule level, to visualize the morphology of aggregates formed by both constructs, thioflavin T (ThT) fluorescence to follow the aggregation kinetics, and circular dichroism (CD) spectroscopy to characterize the secondary structure of the constructs. The ThT fluorescence data showed that the AP-hairpin aggregation kinetics is insensitive to the external environment such as ionic strength and pH contrary to the monomers the kinetics of which depends dramatically on the ionic strength and pH. The AFM topographic imaging revealed that AP--hairpins primarily assemble into globular aggregates, whereas linear fibrils are primary assemblies of the monomers suggesting that both constructs follow different aggregation pathways during the self-assembly. These morphological differences are in line with the AFM force spectroscopy experiments and CD spectroscopy measurements, suggesting that the AP-hairpin is structurally rigid regardless of changes of environmental factors. äRole of monomer arrangement in the amyloid self-assembly (epmc).pdf DeepDyve Pubget Overpricing