scholarly journals β-Sheet Core of Tau Paired Helical Filaments Revealed by Solid-State NMR

2012 ◽  
Vol 134 (34) ◽  
pp. 13982-13989 ◽  
Author(s):  
Venita Daebel ◽  
Subashchandrabose Chinnathambi ◽  
Jacek Biernat ◽  
Martin Schwalbe ◽  
Birgit Habenstein ◽  
...  
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Paired Helical Filaments ◽  
Β Sheet

Verification of the C-terminal intramolecular β-sheet in Aβ42 aggregates using solid-state NMR: Implications for potent neurotoxicity through the formation of radicals

2008 ◽  
Vol 18 (11) ◽  
pp. 3206-3210 ◽  
Author(s):  
Yuichi Masuda ◽  
Satoko Uemura ◽  
Azusa Nakanishi ◽  
Ryutaro Ohashi ◽  
K. Takegoshi ◽  
...  
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Β Sheet

Solid-State NMR Spectroscopy of Functional Amyloid from a Fungal Hydrophobin: A Well-Ordered β-Sheet Core Amidst Structural Heterogeneity

2012 ◽  
Vol 51 (50) ◽  
pp. 12621-12625 ◽  
Author(s):  
Vanessa K. Morris ◽  
Rasmus Linser ◽  
Karyn L. Wilde ◽  
Anthony P. Duff ◽  
Margaret Sunde ◽  
...  
Keyword(s):  
Solid State ◽  
Nmr Spectroscopy ◽  
Solid State Nmr ◽  
Structural Heterogeneity ◽  
Functional Amyloid ◽  
Solid State Nmr Spectroscopy ◽  
Β Sheet

Parallel β-Sheet Structure of Alanine Tetrapeptide in the Solid State As Studied by Solid-State NMR Spectroscopy

2016 ◽  
Vol 120 (34) ◽  
pp. 8932-8941 ◽  
Author(s):  
Tetsuo Asakura ◽  
Kumiko Horiguchi ◽  
Akihiro Aoki ◽  
Yugo Tasei ◽  
Akira Naito
Keyword(s):  
Solid State ◽  
Nmr Spectroscopy ◽  
Solid State Nmr ◽  
Solid State Nmr Spectroscopy ◽  
Sheet Structure ◽  
Β Sheet

scholarly journals Molecular structure of monomorphic peptide fibrils within a kinetically trapped hydrogel network

2015 ◽  
Vol 112 (32) ◽  
pp. 9816-9821 ◽  
Author(s):  
Katelyn Nagy-Smith ◽  
Eric Moore ◽  
Joel Schneider ◽  
Robert Tycko
Keyword(s):  
Solid State ◽  
Self Assembly ◽  
Solid State Nmr ◽  
De Novo ◽  
High Fidelity ◽  
Nmr Data ◽  
Hydrogel Network ◽  
Peptide Fibrils ◽  
Hairpin Conformation ◽  
Β Sheet

Most, if not all, peptide- and protein-based hydrogels formed by self-assembly can be characterized as kinetically trapped 3D networks of fibrils. The propensity of disease-associated amyloid-forming peptides and proteins to assemble into polymorphic fibrils suggests that cross-β fibrils comprising hydrogels may also be polymorphic. We use solid-state NMR to determine the molecular and supramolecular structure of MAX1, a de novo designed gel-forming peptide, in its fibrillar state. We find that MAX1 adopts a β-hairpin conformation and self-assembles with high fidelity into a double-layered cross-β structure. Hairpins assemble with an in-register Syn orientation within each β-sheet layer and with an Anti orientation between layers. Surprisingly, although the MAX1 fibril network is kinetically trapped, solid-state NMR data show that fibrils within this network are monomorphic and most likely represent the thermodynamic ground state. Intermolecular interactions not available in alternative structural arrangements apparently dictate this monomorphic behavior.

Difference in the structures of alanine tri- and tetra-peptides with antiparallel β-sheet assessed by X-ray diffraction, solid-state NMR and chemical shift calculations by GIPAW

Biopolymers ◽  
2013 ◽  
Vol 101 (1) ◽  
pp. 13-20 ◽  
Author(s):  
Tetsuo Asakura ◽  
Koji Yazawa ◽  
Kumiko Horiguchi ◽  
Furitsu Suzuki ◽  
Yusuke Nishiyama ◽  
...  
Keyword(s):  
Solid State ◽  
Chemical Shift ◽  
Solid State Nmr ◽  
X Ray Diffraction ◽  
X Ray ◽  
Β Sheet ◽  
Chemical Shift Calculations

scholarly journals Solid-State NMR Studies Reveal Native-like β-Sheet Structures in Transthyretin Amyloid

Biochemistry ◽  
2016 ◽  
Vol 55 (37) ◽  
pp. 5272-5278 ◽  
Author(s):  
Kwang Hun Lim ◽  
Anvesh K. R. Dasari ◽  
Ivan Hung ◽  
Zhehong Gan ◽  
Jeffery W. Kelly ◽  
...  
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Nmr Studies ◽  
Β Sheet
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