Spider prey-wrapping silk is an α-helical coiled-coil/β-sheet hybrid nanofiber

2018 ◽  
Vol 54 (76) ◽  
pp. 10746-10749 ◽  
Author(s):  
B. Addison ◽  
D. Onofrei ◽  
D. Stengel ◽  
B. Blass ◽  
B. Brenneman ◽  
...  
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Coiled Coil ◽  
Secondary Structures ◽  
Random Coil ◽  
Hybrid Nanofiber ◽  
Β Sheet ◽  
Total P

Solid-State NMR results on 13C-Ala/Ser and 13C-Val enriched Argiope argentata prey-wrapping silk show that native, freshly spun aciniform silk nanofibers are dominated by α-helical (∼50% total) and random-coil (∼35% total) secondary structures, with minor β-sheet nanocrystalline domains (∼15% total).

In situ microscopic studies on the structures and phase behaviors of SF/PEG films using solid-state NMR and Raman imaging

2016 ◽  
Vol 18 (24) ◽  
pp. 16353-16360 ◽  
Author(s):  
Congheng Chen ◽  
Ting Yao ◽  
Sidong Tu ◽  
Weijie Xu ◽  
Yi Han ◽  
...  
Keyword(s):  
Phase Separation ◽  
Solid State Nmr ◽  
Random Coil ◽  
Rich Domain ◽  
Microscopic Studies ◽  
Helix Conformation ◽  
Phase Behaviors ◽  
Protein Rich ◽  
Β Sheet

SF was incompatible with PEG in some extent, and the phase separation took place in their blend film. The conformation of SF in the interface between SF and PEG was changed to the β-sheet, while that in the protein-rich domain remained in the random coil and/or helix conformation.

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

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

A comparison of centrifugally-spun and electrospun regenerated silk fibroin nanofiber structures and properties

RSC Advances ◽  
2015 ◽  
Vol 5 (119) ◽  
pp. 98553-98558 ◽  
Author(s):  
Chen Liu ◽  
Jiaqi Sun ◽  
Min Shao ◽  
Bin Yang
Keyword(s):  
Thermal Properties ◽  
Silk Fibroin ◽  
Secondary Structures ◽  
Random Coil ◽  
Structures And Properties ◽  
Regenerated Silk Fibroin ◽  
Centrifugal Spinning ◽  
Β Sheet

Centrifugal spinning converts the conformation of silk fibroin from random coil to β-sheet more easily than electrospinning, which results in fiber differences on secondary structures, orientation and thermal properties.

scholarly journals Verification of the Intermolecular Parallel β-Sheet in E22K-Aβ42 Aggregates by Solid-State NMR Using Rotational Resonance: Implications for the Supramolecular Arrangement of the Toxic Conformer of Aβ42

2008 ◽  
Vol 72 (8) ◽  
pp. 2170-2175 ◽  
Author(s):  
Yuichi MASUDA ◽  
Azusa NAKANISHI ◽  
Ryutaro OHASHI ◽  
Kiyonori TAKEGOSHI ◽  
Takahiko SHIMIZU ◽  
...  
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Rotational Resonance ◽  
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.

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