scholarly journals Analysis of repetitive amino acid motifs reveals the essential features of spider dragline silk proteins

PLoS ONE ◽  
2017 ◽  
Vol 12 (8) ◽  
pp. e0183397 ◽  
Author(s):  
Ali D. Malay ◽  
Kazuharu Arakawa ◽  
Keiji Numata
Keyword(s):  
Amino Acid ◽  
Silk Proteins ◽  
Dragline Silk ◽  
Spider Dragline Silk

Amino acid analysis of spider dragline silk using 1H NMR

2013 ◽  
Vol 440 (2) ◽  
pp. 150-157 ◽  
Author(s):  
Xiangyan Shi ◽  
Gregory P. Holland ◽  
Jeffery L. Yarger
Keyword(s):  
Amino Acid ◽  
1H Nmr ◽  
Amino Acid Analysis ◽  
Dragline Silk ◽  
Spider Dragline Silk

scholarly journals Methionine in a protein hydrophobic core drives tight interactions required for assembly of spider silk

2019 ◽  
Vol 10 (1) ◽  
Author(s):  
Julia C. Heiby ◽  
Benedikt Goretzki ◽  
Christopher M. Johnson ◽  
Ute A. Hellmich ◽  
Hannes Neuweiler
Keyword(s):  
Amino Acid ◽  
Spider Silk ◽  
Tight Binding ◽  
Pivotal Role ◽  
Speed Limit ◽  
Hydrophobic Core ◽  
Complex Mechanism ◽  
Silk Proteins ◽  
Dragline Silk ◽  
Amino Acid Methionine

Abstract Web spiders connect silk proteins, so-called spidroins, into fibers of extraordinary toughness. The spidroin N-terminal domain (NTD) plays a pivotal role in this process: it polymerizes spidroins through a complex mechanism of dimerization. Here we analyze sequences of spidroin NTDs and find an unusually high content of the amino acid methionine. We simultaneously mutate all methionines present in the hydrophobic core of a spidroin NTD from a nursery web spider’s dragline silk to leucine. The mutated NTD is strongly stabilized and folds at the theoretical speed limit. The structure of the mutant is preserved, yet its ability to dimerize is substantially impaired. We find that side chains of core methionines serve to mobilize the fold, which can thereby access various conformations and adapt the association interface for tight binding. Methionine in a hydrophobic core equips a protein with the capacity to dynamically change shape and thus to optimize its function.

scholarly journals Spider dragline silk proteins in transgenic tobacco leaves: accumulation and field production

2004 ◽  
Vol 2 (5) ◽  
pp. 431-438 ◽  
Author(s):  
Rima Menassa ◽  
Hong Zhu ◽  
Costas N. Karatzas ◽  
Anthoula Lazaris ◽  
Alex Richman ◽  
...  
Keyword(s):  
Transgenic Tobacco ◽  
Silk Proteins ◽  
Dragline Silk ◽  
Tobacco Leaves ◽  
Spider Dragline Silk ◽  
Field Production

scholarly journals Novel Assembly Properties of Recombinant Spider Dragline Silk Proteins

2004 ◽  
Vol 14 (22) ◽  
pp. 2070-2074 ◽  
Author(s):  
Daniel Huemmerich ◽  
Thomas Scheibel ◽  
Fritz Vollrath ◽  
Shulamit Cohen ◽  
Uri Gat ◽  
...  
Keyword(s):  
Silk Proteins ◽  
Dragline Silk ◽  
Spider Dragline Silk

Scalable Spider Silk Inspired Materials with High Extensibility and Super Toughness

2021 ◽  
Vol 893 ◽  
pp. 31-35
Author(s):  
Jin Lian Hu ◽  
Yuan Zhang Jiang ◽  
Lin Gu
Keyword(s):  
Chemical Synthesis ◽  
Spider Silk ◽  
Helical Structure ◽  
Silk Proteins ◽  
Dragline Silk ◽  
Spider Dragline Silk ◽  
Argiope Trifasciata ◽  
Chemical Synthesis Route ◽  
Β Sheet ◽  
Huge Challenge

Spiders silks have extraordinary strength and toughness simultaneously, thus has become dreamed materials by scientists and industries. Although there have been tremendous attempts to prepare fibers from genetically manufacture spider silk proteins, however, it has been still a huge challenge because of tedious procedure and high cost. Here, a facile spider-silk-mimicking strategy is reported for preparing highly scratchable polymers and supertough fibers from chemical synthesis route. Polymer films with high extensibility (>1200%) and supertough fibers (~387 MJ m-3) are achieved by introducing polypeptides with β-sheet and α-helical structure in polyureathane/urea polymers. Notabley,the toughness of the fiber is more than twice the reported value of a normal spider dragline silk, and comparable with the toughest spider silk, aciniform silk of Argiope trifasciata.

scholarly journals Microbial production of amino acid-modified spider dragline silk protein with intensively improved mechanical properties

2016 ◽  
Vol 46 (6) ◽  
pp. 552-558 ◽  
Author(s):  
Haibo Zhang ◽  
Fengli Zhou ◽  
Xinglin Jiang ◽  
Mingle Cao ◽  
Shilu Wang ◽  
...  
Keyword(s):  
Mechanical Properties ◽  
Amino Acid ◽  
Microbial Production ◽  
Silk Protein ◽  
Dragline Silk ◽  
Spider Dragline Silk

scholarly journals Antheraea pernyiSilk Fiber: A Potential Resource for Artificially Biospinning Spider Dragline Silk

2010 ◽  
Vol 2010 ◽  
pp. 1-8 ◽  
Author(s):  
Yaopeng Zhang ◽  
Hongxia Yang ◽  
Huili Shao ◽  
Xuechao Hu
Keyword(s):  
Mechanical Properties ◽  
Optical Orientation ◽  
Silk Proteins ◽  
Dragline Silk ◽  
Silk Fibers ◽  
Spider Dragline Silk ◽  
Initial Modulus ◽  
Sheet Structure ◽  
Potential Resource ◽  
Breaking Energy

The outstanding properties of spider dragline silk are likely to be determined by a combination of the primary sequences and the secondary structure of the silk proteins.Antheraea pernyisilk has more similar sequences to spider dragline silk than the silk from its domestic counterpart,Bombyx mori. This makes it much potential as a resource for biospinning spider dragline silk. This paper further verified its possibility as the resource from the mechanical properties and the structures of theA. pernyisilks prepared by forcible reeling. It is surprising that the stress-strain curves of theA. pernyifibers show similar sigmoidal shape to those of spider dragline silk. Under a controlled reeling speed of 95 mm/s, the breaking energy was1.04×105 J/kg, the tensile strength was 639 MPa and the initial modulus was 9.9 GPa. It should be noted that this breaking energy of theA. pernyisilk approaches that of spider dragline silk. The tensile properties, the optical orientation and theβ-sheet structure contents of the silk fibers are remarkably increased by raising the spinning speeds up to 95 mm/s.

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