scholarly journals Supercontraction of spider dragline silk for humidity sensing

2021 ◽  
Author(s):  
Yu Zhang ◽  
xuhao ji ◽  
Zhihai Liu ◽  
Min Zhang ◽  
hongru song ◽  
...  
Keyword(s):  
Dragline Silk ◽  
Humidity Sensing ◽  
Spider Dragline Silk

SPIDER DRAGLINE SILK: CORRELATED AND MOSAIC EVOLUTION IN HIGH-PERFORMANCE BIOLOGICAL MATERIALS

Evolution ◽  
2006 ◽  
Vol 60 (12) ◽  
pp. 2539 ◽  
Author(s):  
Brook O. Swanson ◽  
Todd A. Blackledge ◽  
Adam P. Summers ◽  
Cheryl Y. Hayashi
Keyword(s):  
High Performance ◽  
Biological Materials ◽  
Dragline Silk ◽  
Spider Dragline Silk ◽  
Mosaic Evolution

Programmable Contractile Actuations of Twisted Spider Dragline Silk Yarns

2021 ◽  
Author(s):  
Lizhong Dong ◽  
Jian Qiao ◽  
Yulong Wu ◽  
Ming Ren ◽  
Yulian Wang ◽  
...  
Keyword(s):  
Dragline Silk ◽  
Spider Dragline Silk

Spider Dragline Silk

1999 ◽  
Vol 39 (4) ◽  
pp. 643-653 ◽  
Author(s):  
STEVEN B. WARNER ◽  
MALCOLM POLK ◽  
KARL JACOB
Keyword(s):  
Dragline Silk ◽  
Spider Dragline Silk

Supercontraction in Nephila spider dragline silk – Relaxation into equilibrium state

Polymer ◽  
2011 ◽  
Vol 52 (26) ◽  
pp. 6056-6060 ◽  
Author(s):  
Roxana Ene ◽  
Periklis Papadopoulos ◽  
Friedrich Kremer
Keyword(s):  
Equilibrium State ◽  
Dragline Silk ◽  
Spider Dragline Silk

Artificial spider silk is smart like natural one: having humidity-sensitive shape memory with superior recovery stress

2019 ◽  
Vol 3 (11) ◽  
pp. 2472-2482 ◽  
Author(s):  
Harun Venkatesan ◽  
Jianming Chen ◽  
Haiyang Liu ◽  
Yoonjung Kim ◽  
Sungsoo Na ◽  
...  
Keyword(s):  
Shape Memory ◽  
Spider Silk ◽  
Recovery Stress ◽  
Dragline Silk ◽  
Spider Dragline Silk ◽  
Shape Memory Behaviour

Inspired by supercontraction, the recombinant spider dragline silk displayed humidity-responsive shape memory behaviour with impressive recovery stress.

Raman Spectroscopic Evidence for Side-Chain Unfolding in Spider Dragline Silk under Tensile Deformation

2005 ◽  
Vol 874 ◽  
Author(s):  
Xiaojun He ◽  
Michael S. Ellison ◽  
Jacqueline M. Palmer
Keyword(s):  
Structural Changes ◽  
Tensile Deformation ◽  
Raman Band ◽  
Side Chain ◽  
Dragline Silk ◽  
Spider Dragline Silk ◽  
Raman Spectroscopic ◽  
Lateral Coupling ◽  
Silk Peptide ◽  
Random Configuration

AbstractIn-situ Ramanspectra were collected on the N. clavipes spider dragline silk under a tensile deformation rate of 15mm/min. The most prominent features on the spectra were due to those bands near 1100 cm-1, which present as a sensitive probe to structural changes associated with side-chains of silk peptide. A downshift of Raman bands at 1095 cm-1 and 1089 cm-1 was detected with increasing strain. Furthermore, an increase in the intensity of the Raman band at 1062 cm-1 due to the vibration of trans structure without lateral coupling was prominent at certain strain levels. This was interpreted in terms of a morphology transition from the random configuration to the trans conformation modulated by the reorganization of the hydrogen bonding among the side-chain.

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.

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