Dimerization of the Conserved N-Terminal Domain of a Spider Silk Protein Controls the Self-Assembly of the Repetitive Core Domain

2017 ◽  
Vol 18 (8) ◽  
pp. 2521-2528 ◽  
Author(s):  
Joschka Bauer ◽  
Thomas Scheibel
Keyword(s):  
Self Assembly ◽  
Spider Silk ◽  
Silk Protein ◽  
The Self ◽  
Core Domain ◽  
Terminal Domain ◽  
Spider Silk Protein

scholarly journals A directed self-assembly quasi-spider silk protein expressed in Pichia pastoris

2017 ◽  
Vol 32 (2) ◽  
pp. 451-461 ◽  
Author(s):  
Bin Liu ◽  
Tao Wang ◽  
Liyan Xiao ◽  
Guilan Zhang ◽  
Guangshen Li ◽  
...  
Keyword(s):  
Pichia Pastoris ◽  
Self Assembly ◽  
Spider Silk ◽  
Silk Protein ◽  
Spider Silk Protein

An Essential Role for the C-Terminal Domain of A Dragline Spider Silk Protein in Directing Fiber Formation

2006 ◽  
Vol 7 (6) ◽  
pp. 1790-1795 ◽  
Author(s):  
Shmulik Ittah ◽  
Shulamit Cohen ◽  
Shai Garty ◽  
Daniel Cohn ◽  
Uri Gat
Keyword(s):  
Essential Role ◽  
Spider Silk ◽  
Fiber Formation ◽  
Silk Protein ◽  
Terminal Domain ◽  
Spider Silk Protein

NMR assignments of a dynamically perturbed and dimerization inhibited N-terminal domain variant of a spider silk protein from E. australis

2019 ◽  
Vol 14 (1) ◽  
pp. 67-71
Author(s):  
Benedikt Goretzki ◽  
Julia C. Heiby ◽  
Carolin Hacker ◽  
Hannes Neuweiler ◽  
Ute A. Hellmich
Keyword(s):  
Spider Silk ◽  
Nmr Assignments ◽  
Silk Protein ◽  
Terminal Domain ◽  
Spider Silk Protein ◽  
Domain Variant

Self-Assembly from Low Dimension to Higher Conformation of GGX Motif in Spider Silk Protein

2009 ◽  
Vol 5 (4) ◽  
pp. 457-464 ◽  
Author(s):  
Qinghan Zhou ◽  
Juan Lin ◽  
Feng Yuan ◽  
Zhaoyang Ye ◽  
Feng Qiu ◽  
...  
Keyword(s):  
Self Assembly ◽  
Spider Silk ◽  
Silk Protein ◽  
Low Dimension ◽  
Spider Silk Protein

scholarly journals Presence of β-Turn Structure in Recombinant Spider Silk Dissolved in Formic Acid Revealed with NMR

Molecules ◽  
2022 ◽  
Vol 27 (2) ◽  
pp. 511
Author(s):  
Yu Suzuki ◽  
Takanori Higashi ◽  
Takahiro Yamamoto ◽  
Hideyasu Okamura ◽  
Takehiro K. Sato ◽  
...  
Keyword(s):  
Mechanical Properties ◽  
Formic Acid ◽  
Spider Silk ◽  
Chemical Shifts ◽  
Repetitive Sequences ◽  
Silk Protein ◽  
Random Coil ◽  
Oh Groups ◽  
Spider Silk Protein ◽  
Turn Structure

Spider dragline silk is a biopolymer with excellent mechanical properties. The development of recombinant spider silk protein (RSP)-based materials with these properties is desirable. Formic acid (FA) is a spinning solvent for regenerated Bombyx mori silk fiber with excellent mechanical properties. To use FA as a spinning solvent for RSP with the sequence of major ampullate spider silk protein from Araneus diadematus, we determined the conformation of RSP in FA using solution NMR to determine the role of FA as a spinning solvent. We assigned 1H, 13C, and 15N chemical shifts to 32-residue repetitive sequences, including polyAla and Gly-rich regions of RSP. Chemical shift evaluation revealed that RSP is in mainly random coil conformation with partially type II β-turn structure in the Gly-Pro-Gly-X motifs of the Gly-rich region in FA, which was confirmed by the 15N NOE data. In addition, formylation at the Ser OH groups occurred in FA. Furthermore, we evaluated the conformation of the as-cast film of RSP dissolved in FA using solid-state NMR and found that β-sheet structure was predominantly formed.

scholarly journals Interfacial Behavior of Recombinant Spider Silk Protein Parts Reveals Cues on the Silk Assembly Mechanism

Langmuir ◽  
2018 ◽  
Vol 34 (39) ◽  
pp. 11795-11805 ◽  
Author(s):  
Linnea Nilebäck ◽  
Suvi Arola ◽  
Mathias Kvick ◽  
Arja Paananen ◽  
Markus B. Linder ◽  
...  
Keyword(s):  
Spider Silk ◽  
Silk Protein ◽  
Interfacial Behavior ◽  
Assembly Mechanism ◽  
Spider Silk Protein

Glycopolymer Functionalization of Engineered Spider Silk Protein-based Materials for Improved Cell Adhesion

2014 ◽  
Vol 14 (7) ◽  
pp. 936-942 ◽  
Author(s):  
John G. Hardy ◽  
André Pfaff ◽  
Aldo Leal-Egaña ◽  
Axel H. E. Müller ◽  
Thomas R. Scheibel
Keyword(s):  
Cell Adhesion ◽  
Spider Silk ◽  
Silk Protein ◽  
Spider Silk Protein

Interactions of Fibroblasts with Different Morphologies Made of an Engineered Spider Silk Protein

2011 ◽  
Vol 14 (3) ◽  
pp. B67-B75 ◽  
Author(s):  
Aldo Leal-Egaña ◽  
Gregor Lang ◽  
Carolin Mauerer ◽  
Jasmin Wickinghoff ◽  
Michael Weber ◽  
...  
Keyword(s):  
Spider Silk ◽  
Silk Protein ◽  
Spider Silk Protein
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