scholarly journals Quantifying the fraction of glycine and alanine in β-sheet and helical conformations in spider dragline silk using solid-state NMR

2008 ◽  
pp. 5568 ◽  
Author(s):  
Gregory P. Holland ◽  
Janelle E. Jenkins ◽  
Melinda S. Creager ◽  
Randolph V. Lewis ◽  
Jeffery L. Yarger
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Dragline Silk ◽  
Spider Dragline Silk ◽  
Β Sheet

Determining Secondary Structure in Spider Dragline Silk by Carbon−Carbon Correlation Solid-State NMR Spectroscopy

2008 ◽  
Vol 130 (30) ◽  
pp. 9871-9877 ◽  
Author(s):  
Gregory P. Holland ◽  
Melinda S. Creager ◽  
Janelle E. Jenkins ◽  
Randolph V. Lewis ◽  
Jeffery L. Yarger
Keyword(s):  
Solid State ◽  
Nmr Spectroscopy ◽  
Secondary Structure ◽  
Solid State Nmr ◽  
Dragline Silk ◽  
Solid State Nmr Spectroscopy ◽  
Spider Dragline Silk

Solid-state NMR evidence for elastin-like β-turn structure in spider dragline silk

2010 ◽  
Vol 46 (36) ◽  
pp. 6714 ◽  
Author(s):  
Janelle E. Jenkins ◽  
Melinda S. Creager ◽  
Emily B. Butler ◽  
Randolph V. Lewis ◽  
Jeffery L. Yarger ◽  
...  
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Dragline Silk ◽  
Spider Dragline Silk ◽  
Turn Structure

Triggered Morphology Generation in a Biosynthetic Model Spider Dragline Silk Protein

1999 ◽  
Vol 5 (S2) ◽  
pp. 1214-1215
Author(s):  
R. Valluzzi ◽  
S. Szela ◽  
D. Kirschner ◽  
D. Kaplan
Keyword(s):  
Recombinant Dna ◽  
Consensus Sequence ◽  
Water Soluble ◽  
Nephila Clavipes ◽  
Dragline Silk ◽  
Spider Dragline Silk ◽  
Structure Changes ◽  
Methionine Residues ◽  
Recombinant Dna Techniques ◽  
Β Sheet

Recombinant DNA techniques were used to prepare a protein modeled after the consensus sequence of Nephila clavipesspider dragline silk, incorporating methionine residues to serve as redox “triggers”. In addition a water-soluble 27 residue peptide model of the dragline silk consensus amorphous sequence, representing a single amorphous block in the protein sequence, was prepared and characterized to gain additional insight into the behavior of the amorphous phase. X-ray diffraction, electron diffraction, transmission electron microscopy (TEM), and Fourier transform infrared spectroscopy (FTIR) were used to characterize the ability of the recombinant protein to form (β-sheet crystals and the effect of the oxidation state of the redox trigger on crystallinity and noncrystalline order in the sample. The formation of intractable β-sheet crystallites is a major cause of insolubility in proteins that can form this type of secondary structure. Changes in crystallinity were observed when triggered/reduced (insoluble) and untriggered/oxidized (soluble) protein samples were compared.

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
Sign in / Sign up

Export Citation Format

Share Document