نتایج جستجو برای: silk protein

تعداد نتایج: 1242331  

Journal: :Biomacromolecules 2004
Barbara A Lawrence Craig A Vierra Anne M F Moore

Molecular and material properties of major ampullate silk were studied for the cobweb-building black widow spider Latrodectus hesperus. Material properties were measured by stretching the silk to breaking. The strength was 1.0 +/- 0.2 GPa, and the extensibility was 34 +/- 8%. The secondary structure of the major ampullate silk protein was studied using carbon-13 NMR spectroscopy. Alanine underg...

Journal: :Journal of structural biology 2014
Olena S Tokareva Shangchao Lin Matthew M Jacobsen Wenwen Huang Daniel Rizzo David Li Marc Simon Cristian Staii Peggy Cebe Joyce Y Wong Markus J Buehler David L Kaplan

Bioengineered spider silk block copolymers were studied to understand the effect of protein chain length and sequence chemistry on the formation of secondary structure and materials assembly. Using a combination of in vitro protein design and assembly studies, we demonstrate that silk block copolymers possessing multiple repetitive units self-assemble into lamellar microstructures. Additionally...

2018
Sean J Blamires Madeleine Nobbs Penny J Martens I-Min Tso Wei-Tsung Chuang Chung-Kai Chang Hwo-Shuenn Sheu

Variability in spider major ampullate (MA) silk properties at different scales has proven difficult to determine and remains an obstacle to the development of synthetic fibers mimicking MA silk performance. A multitude of techniques may be used to measure multiscale aspects of silk properties. Here we fed five species of Araneoid spider solutions that either contained protein or were protein de...

Journal: :Biomaterials 2006
Yongzhong Wang Hyeon-Joo Kim Gordana Vunjak-Novakovic David L Kaplan

Silks are naturally occurring polymers that have been used clinically as sutures for centuries. When naturally extruded from insects or worms, silk is composed of a filament core protein, termed fibroin, and a glue-like coating consisting of sericin proteins. In recent years, silk fibroin has been increasingly studied for new biomedical applications due to the biocompatibility, slow degradabili...

2016
Nan Qin Shaoqing Zhang Jianjuan Jiang Stephanie Gilbert Corder Zhigang Qian Zhitao Zhou Woonsoo Lee Keyin Liu Xiaohan Wang Xinxin Li Zhifeng Shi Ying Mao Hans A Bechtel Michael C Martin Xiaoxia Xia Benedetto Marelli David L Kaplan Fiorenzo G Omenetto Mengkun Liu Tiger H Tao

Silk protein fibres produced by silkworms and spiders are renowned for their unparalleled mechanical strength and extensibility arising from their high-β-sheet crystal contents as natural materials. Investigation of β-sheet-oriented conformational transitions in silk proteins at the nanoscale remains a challenge using conventional imaging techniques given their limitations in chemical sensitivi...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2010
Xiao-Xia Xia Zhi-Gang Qian Chang Seok Ki Young Hwan Park David L Kaplan Sang Yup Lee

Spider dragline silk is a remarkably strong fiber that makes it attractive for numerous applications. Much has thus been done to make similar fibers by biomimic spinning of recombinant dragline silk proteins. However, success is limited in part due to the inability to successfully express native-sized recombinant silk proteins (250-320 kDa). Here we show that a 284.9 kDa recombinant protein of ...

Journal: :Science 2002
Anthoula Lazaris Steven Arcidiacono Yue Huang Jiang-Feng Zhou Francois Duguay Nathalie Chretien Elizabeth A Welsh Jason W Soares Costas N Karatzas

Spider silks are protein-based "biopolymer" filaments or threads secreted by specialized epithelial cells as concentrated soluble precursors of highly repetitive primary sequences. Spider dragline silk is a flexible, lightweight fiber of extraordinary strength and toughness comparable to that of synthetic high-performance fibers. We sought to "biomimic" the process of spider silk production by ...

2011
Melis Arslan Markus J. Buehler

Silk is an ancient but remarkably strong, extensible and tough material made from simple protein building blocks. Earlier work has shown that the particular molecular geometry of silk with a composite of semi-amorphous and nanocrystalline beta-sheet protein domains provides the structural basis for its characteristic softening-stiffening behavior and remarkable strength at the nanoscale. Yet, a...

Journal: :The journal of physical chemistry. B 2005
Li Zhou Xin Chen Zhengzhong Shao Yufang Huang David P Knight

A protein conformation transition from random coil and/or helical conformation to beta-sheet is known to be central to the process used by silk-spinning spiders and insects to convert concentrated protein solutions to tough insoluble threads. Several factors including pH, metallic ions, shear force, and/or elongational flow can initiate this transition in both spiders and silkworms. Here, we re...

1976
MARK DENNY M. DENNY

1. Determinations were made of several physical properties of the viscid and frame silks of the orb-webs built by the spider Araneus sericatus (Cl.). 2. Both types of silk show a breaking stress of approximately 1 GN/m and an initial resilience of approximately 0-35. 3. The breaking extension ratio of viscid silk (A = 3*00) is much greater than that of frame silk (A = i2s), and the viscid silk ...

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