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10.1016/j.ultramic.2016.03.011 http://scihub22266oqcxt.onion/10.1016/j.ultramic.2016.03.011 C4879610!4879610 !27060278     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27060278 &cmd=llinks): Failed to open stream: HTTP request failed! 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Polymorphism of amyloid fibrils formed by a peptide from the yeast prion protein Sup35: AFM and Tip-Enhanced Raman Scattering studies |pdf=|usr=}}{{27060278 }} gab.com Text Polymorphism of amyloid fibrils formed by a peptide from the yeast prion protein Sup35: AFM and Tip-Enhanced Raman Scattering studies JO: Ultramicroscopy http://www.kidney.de/pget.php?&tw=1&pmid=27060278 #FOAvip Aggregation of prion proteins is the cause of various prion related diseases. The infectious form of prions, amyloid aggregates, exist as multiple strains. The strains are thought to represent structurally different prion protein molecules packed into amyloid aggregates, but the knowledge on the structure of different types of aggregates is limited. Here we report on the use of AFM (Atomic Force Microscopy) and TERS (Tip-Enhanced Raman Scattering) to study morphological heterogeneity and access underlying conformational features of individual amyloid aggregates. Using AFM we identified the morphology of amyloid fibrils formed by the peptide (CGNNQQNY) from the yeast prion protein Sup35 that is critically involved in the aggregation of the full protein. TERS results demonstrate that morphologically different amyloid fibrils are composed of a distinct set of conformations. Fibrils formed at pH 5.6 are composed of a mixture of peptide conformations (?-sheets, random coil and ?-helix) while fibrils formed in pH~2 solution primarily have ?-sheets. Additionally, peak positions in the amide III region of the TERS spectra suggested that peptides have parallel arrangement of ?-sheets for pH~2 fibrils and antiparallel arrangement for fibrils formed at pH 5.6. We also developed a methodology for detailed analysis of the peptide secondary structure by correlating intensity changes of Raman bands in different regions of TERS spectra. Such correlation established that structural composition of peptides is highly localized with large contribution of unordered secondary structures on a fibrillar surface. Twit Text FOAVip Polymorphism of amyloid fibrils formed by a peptide from the yeast prion protein Sup35: AFM and Tip-Enhanced Raman Scattering studies ????Ultramicroscopy http://www.kidney.de/pget.php?&tw=1&pmid=27060278 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27060278 #FOAvip English Wikipedia <ref>{{Cite pmid|27060278 }}</ref> Polymorphism of amyloid fibrils formed by a peptide from the yeast prion protein Sup35: AFM and Tip-Enhanced Raman Scattering studies #MMPMID27060278 Krasnoslobodtsev AV ; Deckert-Gaudig T ; Zhang Y ; Deckert V ; Lyubchenko YL Ultramicroscopy 2016[Jun]; 165 (ä): 26-33 PMID27060278 show ga Aggregation of prion proteins is the cause of various prion related diseases. The infectious form of prions, amyloid aggregates, exist as multiple strains. The strains are thought to represent structurally different prion protein molecules packed into amyloid aggregates, but the knowledge on the structure of different types of aggregates is limited. Here we report on the use of AFM (Atomic Force Microscopy) and TERS (Tip-Enhanced Raman Scattering) to study morphological heterogeneity and access underlying conformational features of individual amyloid aggregates. Using AFM we identified the morphology of amyloid fibrils formed by the peptide (CGNNQQNY) from the yeast prion protein Sup35 that is critically involved in the aggregation of the full protein. TERS results demonstrate that morphologically different amyloid fibrils are composed of a distinct set of conformations. Fibrils formed at pH 5.6 are composed of a mixture of peptide conformations (?-sheets, random coil and ?-helix) while fibrils formed in pH~2 solution primarily have ?-sheets. Additionally, peak positions in the amide III region of the TERS spectra suggested that peptides have parallel arrangement of ?-sheets for pH~2 fibrils and antiparallel arrangement for fibrils formed at pH 5.6. We also developed a methodology for detailed analysis of the peptide secondary structure by correlating intensity changes of Raman bands in different regions of TERS spectra. Such correlation established that structural composition of peptides is highly localized with large contribution of unordered secondary structures on a fibrillar surface. |*Amyloid/chemistry [MESH] |*Prion Proteins/chemistry [MESH] |*Spectrum Analysis, Raman [MESH] |Peptides/chemistry [MESH]Polymorphism of amyloid fibrils formed by a peptide from the yeast pri(epmc).pdf DeepDyve Pubget Overpricing