Log in

Relevant bibliographies by topics / Protein elasticity

Contents

Journal articles
Dissertations / Theses
Books
Book chapters
Conference papers

Academic literature on the topic 'Protein elasticity'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'Protein elasticity.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "Protein elasticity"

1

ZHANG, YONG, LURU DAI, and ZHONG-CAN OU-YANG. "AMINO ACID COMPOSITION-DEPENDENT ELASTICITY OF SPIDER SILK." International Journal of Modern Physics B 18, no. 17n19 (2004): 2516–22. http://dx.doi.org/10.1142/s0217979204025592.

Full text

Abstract:

Spider silk exhibits excellent mechanical features in both toughness and extensibility. In recent years considerable investigations have focused on it. The understanding of spider silk protein is important for the development bionic silk. In this paper, we study by Monte Carlo simulation the force-of-extension property of spider silk proteins as a function of the residue composition for major and minor ampullate glands of typical Araneid orb weaver as well as that for one artificial spider silk. The results are also compared with those from a designed protein whose amino acid composition is un

APA, Harvard, Vancouver, ISO, and other styles

2

Tatham, Arthur S., Larry Hayes, Peter R. Shewry, and Dan W. Urry. "Wheat seed proteins exhibit a complex mechanism of protein elasticity." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1548, no. 2 (2001): 187–93. http://dx.doi.org/10.1016/s0167-4838(01)00232-1.

Full text

APA, Harvard, Vancouver, ISO, and other styles

3

Yang, Qing Bin, and Shou Wu Gao. "The Elasticity of Soybean Protein Fiber Blended Yarn." Advanced Materials Research 322 (August 2011): 275–78. http://dx.doi.org/10.4028/www.scientific.net/amr.322.275.

Full text

Abstract:

Abstract In order to describe the relation between the elasticity and the blended ratio of soybean protein fiber blended yarn, the elasticity of different kinds of blended ratio of soybean protein fiber/polyester and soybean protein fiber/cotton blended yarn was measured. The relation between the elasticity and the blended ratio of blended yarn is determined. The optimum blended ratio is analyzed.

APA, Harvard, Vancouver, ISO, and other styles

4

Dimitrova, Tatiana D., and Fernando Leal-Calderon. "Bulk Elasticity of Concentrated Protein-Stabilized Emulsions." Langmuir 17, no. 11 (2001): 3235–44. http://dx.doi.org/10.1021/la001805n.

Full text

APA, Harvard, Vancouver, ISO, and other styles

5

Lundbæk, Jens A., Pia Birn, Anker J. Hansen, et al. "Regulation of Sodium Channel Function by Bilayer Elasticity." Journal of General Physiology 123, no. 5 (2004): 599–621. http://dx.doi.org/10.1085/jgp.200308996.

Full text

Abstract:

Membrane proteins are regulated by the lipid bilayer composition. Specific lipid–protein interactions rarely are involved, which suggests that the regulation is due to changes in some general bilayer property (or properties). The hydrophobic coupling between a membrane-spanning protein and the surrounding bilayer means that protein conformational changes may be associated with a reversible, local bilayer deformation. Lipid bilayers are elastic bodies, and the energetic cost of the bilayer deformation contributes to the total energetic cost of the protein conformational change. The energetics a

APA, Harvard, Vancouver, ISO, and other styles

6

Leu, Bogdan M., Ahmet Alatas, Harald Sinn, et al. "Protein elasticity probed with two synchrotron-based techniques." Journal of Chemical Physics 132, no. 8 (2010): 085103. http://dx.doi.org/10.1063/1.3332585.

Full text

APA, Harvard, Vancouver, ISO, and other styles

7

Lee, Jonghwi, Christopher W. MacOsko, and Dan W. Urry. "Phase transition and elasticity of protein-based hydrogels." Journal of Biomaterials Science, Polymer Edition 12, no. 2 (2001): 229–42. http://dx.doi.org/10.1163/156856201750180942.

Full text

APA, Harvard, Vancouver, ISO, and other styles

8

Lichtenberg, B., E. M. Mandelkow, T. Hagestedt, and E. Mandelkow. "Structure and elasticity of microtubule-associated protein tau." Nature 334, no. 6180 (1988): 359–62. http://dx.doi.org/10.1038/334359a0.

Full text

APA, Harvard, Vancouver, ISO, and other styles

9

Jacobs, Miranda L., and Neha P. Kamat. "Investigating How Membrane Elasticity Impacts Membrane Protein Folding." Biophysical Journal 116, no. 3 (2019): 25a. http://dx.doi.org/10.1016/j.bpj.2018.11.181.

Full text

APA, Harvard, Vancouver, ISO, and other styles

10

Buehler, Markus. "Hierarchical chemo-nanomechanics of proteins: entropic elasticity, protein unfolding and molecular fracture." Journal of Mechanics of Materials and Structures 2, no. 6 (2007): 1019–57. http://dx.doi.org/10.2140/jomms.2007.2.1019.

Full text

APA, Harvard, Vancouver, ISO, and other styles

Dissertations / Theses on the topic "Protein elasticity"

1

Zinober-Moore, Rebecca C. "Elasticity and mechanical unfolding of globular protein domains." Thesis, University of Leeds, 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.426849.

Full text

APA, Harvard, Vancouver, ISO, and other styles

2

Becker, Nils B. "Sequence dependent elasticity of DNA." Doctoral thesis, [S.l. : s.n.], 2007. http://nbn-resolving.de/urn:nbn:de:swb:14-1186511923001-71752.

Full text

APA, Harvard, Vancouver, ISO, and other styles

3

Toda, Hiroyuki. "Design of Protein Immobilization and Elasticity of Polymer Hydrogels for Cell Culture." 京都大学 (Kyoto University), 2016. http://hdl.handle.net/2433/215569.

Full text

APA, Harvard, Vancouver, ISO, and other styles

4

Kappiyoor, Ravi. "Mechanical Properties of Elastomeric Proteins." Diss., Virginia Tech, 2014. http://hdl.handle.net/10919/54563.

Full text

Abstract:

When we stretch and contract a rubber band a hundred times, we expect the rubber band to fail. Yet our heart stretches and contracts the same amount every two minutes, and does not fail. Why is that? What causes the significantly higher elasticity of certain molecules and the rigidity of others? Equally importantly, can we use this information to design materials for precise mechanical tasks? It is the aim of this dissertation to illuminate key aspects of the answer to these questions, while detailing the work that remains to be done. In this dissertation, particular emphasis is placed on the

APA, Harvard, Vancouver, ISO, and other styles

5

Janovjak, Harald. "Exploring the Mechanical Stability and Visco-elasticity of Membrane Proteins by Single-Molecule Force Measurements." Doctoral thesis, Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2005. http://nbn-resolving.de/urn:nbn:de:swb:14-1135090167025-44737.

Full text

Abstract:

Relatively little is known about the folding and stability of membrane proteins. Conventional thermal or chemical unfolding techniques probe the average behavior of large numbers of molecules and thus cannot resolve co-existing minor and major unfolding pathways and intermediates. Here, I applied single-molecule force measurements based on an atomic force microscope (AFM) to characterize the stability of the membrane protein bacteriorhodopsin (BR). In these mechanical unfolding experiments, an external pulling force played the role of the denaturant and lead to unfolding of the three-dimension

APA, Harvard, Vancouver, ISO, and other styles

6

Bagheri, Mehran. "Intrinsically Disordered Proteins: Mechanics, Assemblies, and Structural Transitions." Thesis, Université d'Ottawa / University of Ottawa, 2017. http://hdl.handle.net/10393/36576.

Full text

Abstract:

Proteins are essential parts of living organisms that initiate and control almost all cellular processes. Despite the widely accepted belief that all functional proteins fold into stable and well-defined three-dimensional (3D) structures mandatory for protein activity, the existence of biologically functional disordered proteins has been increasingly recognized during past two decades. Proteins with inherent structural disorder, commonly known as intrinsically disordered proteins (IDPs), play many roles in a biological context. However, in contrast to their folded counterparts, they are dynami

APA, Harvard, Vancouver, ISO, and other styles

7

Green, Ellen Marie. "Mechanisms of elasticity in elastic proteins." Thesis, University of Exeter, 2012. http://hdl.handle.net/10036/4058.

Full text

Abstract:

This thesis investigates the mechanical properties of the elastic proteins isolated by cyanogen bromide digestion from lamprey cartilages and compares them with the mammalian protein, elastin. Thermomechanical testing and measurements of the effects of hydrophobic solvents on mechanics are used to determine the energetic and entropic contributions to the mechanical properties and the role of solvent interactions. Raman microspectrometry is shown to be a valuable tool in determining the secondary structure of the proteins, their interactions with water and molecular-level effects of mechanical

APA, Harvard, Vancouver, ISO, and other styles

8

Schwarzl, Richard [Verfasser]. "Elasticity of Proteins and Polymers from Molecular Dynamics Simulations / Richard Schwarzl." Berlin : Freie Universität Berlin, 2021. http://d-nb.info/1241117853/34.

Full text

APA, Harvard, Vancouver, ISO, and other styles

9

Menou, Lucas. "Elasticité de capsides virales et défauts topologiques." Thesis, Lyon, 2020. http://www.theses.fr/2020LYSEN038.

Full text

Abstract:

Les différentes propriétés des virus en font des objets intéressants et fascinants. On peut en trouver de différentes structures, avec des méthodes de réplication différentes et ils sont spécifiques à leurs cibles. Ils constituent la plus petite entité auto-assemblée, elle-même encodée par un matériel génétique. Ce génome est protégé par une capside à l'intérieur virus lui-même. La capside est le constituant le plus important d'un virus. Son rôle est de protéger le génome viral des agressions extérieures. De fait, elle peut supporter de hautes contraintes mécaniques ou chimiques externes et/ou

APA, Harvard, Vancouver, ISO, and other styles

10

Borazjani, Ali. "Pathophysiology of Pelvic Organ Prolapse." Cleveland State University / OhioLINK, 2015. http://rave.ohiolink.edu/etdc/view?acc_num=csu1432745397.

Full text

APA, Harvard, Vancouver, ISO, and other styles

Books on the topic "Protein elasticity"

1

Gerry, Simpson. Part III Regimes and Doctrines, Ch.28 Something to do with States. Oxford University Press, 2016. http://dx.doi.org/10.1093/law/9780198701958.003.0029.

Full text

Abstract:

This chapter suggests that the law of sovereignty and statehood tends to be practiced, organized, and theorized around two sets of argument (and a sleight of hand), and that this tendency has produced certain effects on the distribution of political resources in global politics. The first argument is structured around the material and immaterial qualities of statehood, as it maintains that the ‘infinite transition’ discussed by Peter Fitzpatrick is produced partly by the elasticity of the doctrinal ground and partly by the remarkable stability of a very particular and idealized sovereign subje

APA, Harvard, Vancouver, ISO, and other styles

Book chapters on the topic "Protein elasticity"

1

Rauscher, Sarah, and Régis Pomès. "Structural Disorder and Protein Elasticity." In Advances in Experimental Medicine and Biology. Springer US, 2012. http://dx.doi.org/10.1007/978-1-4614-0659-4_10.

Full text

APA, Harvard, Vancouver, ISO, and other styles

2

Gruner, Sol M. "Lipid Membrane Curvature Elasticity and Protein Function." In Biologically Inspired Physics. Springer US, 1991. http://dx.doi.org/10.1007/978-1-4757-9483-0_11.

Full text

APA, Harvard, Vancouver, ISO, and other styles

3

Gruner, Sol M. "Coupling between Bilayer Curvature Elasticity and Membrane Protein Activity." In Advances in Chemistry. American Chemical Society, 1994. http://dx.doi.org/10.1021/ba-1994-0235.ch007.

Full text

APA, Harvard, Vancouver, ISO, and other styles

4

Sackmann, Enrico, H. P. Duwe, K. Zeman, and A. Zilker. "Elasticity, Structure and Dynamics of Cell Plasma Membrane and Biological Functions." In Structure and Dynamics of Nucleic Acids, Proteins, and Membranes. Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-5308-9_19.

Full text

APA, Harvard, Vancouver, ISO, and other styles

5

Urry, D. W., T. Hugel, M. Seitz, et al. "Ideal Protein Elasticity: The Elastin Models." In Elastomeric Proteins. Cambridge University Press, 2003. http://dx.doi.org/10.1017/cbo9780511546327.006.

Full text

APA, Harvard, Vancouver, ISO, and other styles

6

Lei, Hongxing, Jiya Sun, Enoch P. Baldwin, David J. Segal, and Yong Duan. "Conformational Elasticity can Facilitate TALE–DNA Recognition." In Advances in Protein Chemistry and Structural Biology. Elsevier, 2014. http://dx.doi.org/10.1016/b978-0-12-800168-4.00009-3.

Full text

APA, Harvard, Vancouver, ISO, and other styles

7

Pabst, Georg. "Coupling Membrane Elasticity and Structure to Protein Function." In Advances in Planar Lipid Bilayers and Liposomes. Elsevier, 2013. http://dx.doi.org/10.1016/b978-0-12-411515-6.00004-7.

Full text

APA, Harvard, Vancouver, ISO, and other styles

8

Ben-Shaul, A. "Molecular Theory of Chain Packing, Elasticity and Lipid-Protein Interaction in Lipid Bilayers." In Handbook of Biological Physics. Elsevier, 1995. http://dx.doi.org/10.1016/s1383-8121(06)80024-2.

Full text

APA, Harvard, Vancouver, ISO, and other styles

9

Erman, Burak, and James E. Mark. "Bioelastomers." In Structures and Properties of Rubberlike Networks. Oxford University Press, 1997. http://dx.doi.org/10.1093/oso/9780195082371.003.0017.

Full text

Abstract:

There are a variety of biopolymeric materials which exhibit rubberlike elasticity. This is perhaps to be expected when one recalls that most biopolymers are randomly coiled chains with considerable flexibility, and that they are frequently covalently cross-linked or have sufficient numbers of aggregated units to exist in network structures. One very large group of plant materials, the polysaccharides, are in this category, and they do require some elastomeric properties in their functioning. In many of these cases, however, the cross-linking is there primarily for a secondary purpose, such as preventing solubility. When swollen with water or aqueous solutions, such polysaccharides form gels which do exhibit the high deformability and recoverability that are the hallmarks of rubberlike elasticity. Not surprisingly, however, relatively few mechanical property measurements have been carried out to characterize the structures of these gels. The bioelastomers occurring in animals, including vertebrates and mammals, however, are there specifically for their rubberlike elasticity. They are vital, for example, for the functioning of skin, arteries and veins, and much of the lung and heart tissue. Since they are produced by the ribosome “factories” in the body, they are proteins. Thus, the major focus of this chapter is on those proteins specifically designed to function as bioelastomers. It is useful to summarize some general information on bioelastomers that is presented elsewhere. Even with the temporary restriction to bioelastomers which are proteins, there is an almost staggering variety of interesting materials. For example, there is elastin in vertebrates (including mammals) resilin in insects abductin in mollusks, arterial elastomer in octopuses, circulatory and locomotional proteins in cephalopods, and viscid silk in spider webs. Since they are mammals, polymer scientists and engineers who are interested in bioelastomers have focused heavily on elastin! Any materials of this type, however, are worth studying in their own right, to learn more about rubberlike elasticity and biological function. Such studies should also provide guidance on how Nature might be mimicked by synthetic chemists, to produce better nonbiological elastomers.

APA, Harvard, Vancouver, ISO, and other styles

10

Bulcsu, Remenyik, Cem Yesilyurt, and Ali Bagdadi. "Alternative Suggestion for the Sustainability of Tourism During Coronavirus Breakout." In Handbook of Research on the Impacts and Implications of COVID-19 on the Tourism Industry. IGI Global, 2021. http://dx.doi.org/10.4018/978-1-7998-8231-2.ch039.

Full text

Abstract:

It was once again seen during the COVID-19 epidemic how demand elasticity is in the tourism sector and how fragile the sector is. One of the most affected sectors by the pandemic was the tourism sector. Due to the restrictions imposed by governments and the measures taken to protect the health of the people, the tourism sector has suffered severely, and many tourism businesses have suffered financial damage in this long process and have had to go bankrupt by not being able to maintain their business. The situation has revealed the importance of sustainability and showed the necessity of ensuring the continuity of business life for tourism enterprises. It has also revealed the importance of sustainability for the tourism sector, which adheres to mass tourism and does not care about other alternative tourism types. In this context, how ready is the tourism sector for crises? Could these crises be responded to with new destinations and new tourism products? Thus, it seems important to consider sustainable tourism and alternative tourism types.

APA, Harvard, Vancouver, ISO, and other styles

Conference papers on the topic "Protein elasticity"

1

Ruggiero, Michael T., and Timothy M. Korter. "Measuring protein elasticity with terahertz spectroscopy." In 2016 41st International Conference on Infrared, Millimeter, and Terahertz waves (IRMMW-THz). IEEE, 2016. http://dx.doi.org/10.1109/irmmw-thz.2016.7758346.

Full text

APA, Harvard, Vancouver, ISO, and other styles

2

Keten, Sinan, and Markus J. Buehler. "Elasticity and Strength of Beta-Sheet Protein Materials: Geometric Confinement and Size Effects." In ASME 2009 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2009. http://dx.doi.org/10.1115/sbc2009-205464.

Full text

Abstract:

Elasticity and strength of proteins influence their biological functions. Under external forces, many proteins exhibit entropic elasticity with a characteristic stiffening elastic behavior and unravel due to the rupture of interstrand H-bonds. We develop a fracture mechanics based theoretical framework that considers the free energy competition between entropic elasticity of polypeptide chains and rupture of peptide hydrogen bonds, which we use here to provide an explanation for the intrinsic strength limit of protein domains at vanishing rates [1, 2]. Our analysis predicts that individual pro

APA, Harvard, Vancouver, ISO, and other styles

3

Efstathiou, S., M. Korsnes, A. Møller Gabrielsen, et al. "1. Investigating the elasticity of meat consumption for climate mitigation: 4Rs for responsible meat use." In 6th EAAP International Symposium on Energy and Protein Metabolism and Nutrition. Wageningen Academic Publishers, 2019. http://dx.doi.org/10.3920/978-90-8686-892-6_1.

Full text

APA, Harvard, Vancouver, ISO, and other styles

4

Le, Victoria, Hiromi Yanagisawa, and Jessica Wagenseil. "Characterization of Cardiac Function and Arterial Mechanics During Early Postnatal Development in Fibulin-5 Null Mice." In ASME 2013 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2013. http://dx.doi.org/10.1115/sbc2013-14282.

Full text

Abstract:

Fibulin-5 is an extracellular matrix protein that interacts with other proteins during a complex process that results in elastic fiber formation from the elastin precursor, tropoelastin [1]. Elastic fibers are an important component of tissues requiring elasticity, including large arteries, lungs and skin. In mice lacking fibulin-5 ( Fbln5−/−), these tissues contain disorganized elastic fibers and exhibit decreased elasticity [2]. The phenotype of Fbln5−/− mice is similar to that of humans with cutis laxa, a connective tissue disorder characterized by loose skin and narrow arteries with reduce

APA, Harvard, Vancouver, ISO, and other styles

5

Purohit, Prashant K. "Fibrin Networks Sustain Large Extensions Due to Unfolding Proteins." In ASME 2010 First Global Congress on NanoEngineering for Medicine and Biology. ASMEDC, 2010. http://dx.doi.org/10.1115/nemb2010-13125.

Full text

Abstract:

Blood clots and thrombi consist primarily of a mesh of branched fibers made of the protein fibrin. We show how these networks give rise to the remarkable extensibility and elasticity of blood clots by determining structural and mechanical properties of the clot at the network, fiber, and molecular levels. The force required to stretch a clot initially rises almost linearly and is accompanied by a dramatic decrease in the clot volume. These macroscopic changes are accompanied by fiber alignment and bundling following forced protein unfolding. We develop constitutive models to integrate observat

APA, Harvard, Vancouver, ISO, and other styles

6

Espinosa, Gabriela, Lisa Bennett, William Gardner, and Jessica Wagenseil. "The Effects of Extracellular Matrix Protein Insufficiency and Treatment on the Stiffness of Arterial Smooth Muscle Cells." In ASME 2013 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2013. http://dx.doi.org/10.1115/sbc2013-14131.

Full text

Abstract:

Increased arterial stiffness is directly correlated with hypertension and cardiovascular disease. Stiffness of the conducting arteries is largely determined by the extracellular matrix (ECM) proteins in the wall, such as collagen and elastin, produced by the smooth muscle cells (SMCs) found in the medial layer. Elastin is deposited as soluble tropoelastin and is later crosslinked into elastin fibers. Newborn mice lacking the elastin protein ( Eln−/−) have increased arterial wall stiffness and SMCs with altered proliferation, migration and morphology [1]. Vessel elasticity is also mediated by o

APA, Harvard, Vancouver, ISO, and other styles

7

Lakkaraju, Sirish Kaushik, and Wonmuk Hwang. "Length and Sequence Dependence of the Elasticity of Alpha Helices and Coiled-Coils." In ASME 2009 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2009. http://dx.doi.org/10.1115/sbc2009-206252.

Full text

Abstract:

Fibrous proteins made by α-helices, one of the most elementary protein secondary structures, have various mechanical roles in a sub cellular environment. An α-helix is wound in a right-handed fashion due to hydrogen bonding between the C=O and the N-H atoms across every i and i+4th residues in the polypeptide chain. Previous approaches characterizing mechanical properties of α-helices treated them as homogenous and linear elastic rods. Stiffness is typically expressed in terms of persistence length lp (∼100nm from Kb∼3×10−28 Nm2, lp = Kb/kT: Kb, the bending stiffness, k the Boltzmann constant

APA, Harvard, Vancouver, ISO, and other styles

8

Karpov, Eduard. "Random Sampling Monte-Carlo Approach to Studying Entropic Elasticity Properties of Cell Proteins and Lipids." In ASME 2010 First Global Congress on NanoEngineering for Medicine and Biology. ASMEDC, 2010. http://dx.doi.org/10.1115/nemb2010-13271.

Full text

Abstract:

An efficient numerical Monte-Carlo method is proposed for the estimation of the entropic contribution to the elastic properties of cell protein and lipid chain biomolecules. Specific load-extension curves are obtained numerically for a group of molecules with degenerate potential energy profiles. Spread of the linear elastic regimes and dependence on the molecular weight and geometric parameters of the molecules are discussed.

APA, Harvard, Vancouver, ISO, and other styles

9

Sun, Hyung Jin, Yunjie Wang, and Katherine Yanhang Zhang. "Changes in the Mechanical Properties of Arterial Elastin With Cholesterol Effect." In ASME 2013 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2013. http://dx.doi.org/10.1115/sbc2013-14591.

Full text

Abstract:

Elastin is a protein in the extracellular matrix that provides critical mechanical properties of elasticity and extensibility to many connective tissues, including arteries. Such properties of elastin allow arteries to accommodate deformations encountered during physiological functions. Elastin is subjected to changes in mechanical properties upon exposure to various chemical environments. Elastin is a hydrophobic protein, which makes it an attractive site for the deposition of hydrophobic ligands such as cholesterol [1]. Cholesterol is a type of lipid that gradually builds up along arterial w

APA, Harvard, Vancouver, ISO, and other styles

10

Munro, Troy, Changhu Xing, Andrew Marquette, Heng Ban, Cameron Copeland, and Randolph Lewis. "Description of Test Setup and Approach to Measure Thermal Properties of Natural and Synthetic Spider Silks at Cryogenic Temperatures." In ASME 2013 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 2013. http://dx.doi.org/10.1115/imece2013-66630.

Full text

Abstract:

Spider silk is well-known for its exceptional mechanical properties, such as strength, elasticity and flexibility. Recently, it has been reported that dragline silk from a Nephila clavipes also has an exceptionally high thermal conductivity, comparable to copper when the fiber is stretched. Synthetic spider silks have been spun from spider silk proteins produced in transgenic sources, and their production process has the optimization potential to have properties similar to or better than the natural spider silk. There is interest to measure the thermal properties of natural and synthetic silk

APA, Harvard, Vancouver, ISO, and other styles

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!