Proteins mechanical properties

Rising A, et al. (2005) Spider Silk Proteins—Mechanical Property and Gene Sequence. Zoological science. 22 p. 273-81. 

Rising, A., Nimmervoll, H., Grip, S., Fernandez-Arias, A., Storckenfeldt, E., ICnight, D. R, Vollrath, F., and Engstrom, W. 2005. Spider silk proteins—Mechanical property and gene sequence. Zoolog Sci, 22, 273-81. 

Biomechanical Machines. The mechanical properties of fibrous polypeptides could be put to use for the commercial production of fibers (qv) that are more elastic and resiUent than available synthetics (see Silk). The biochemical properties of proteins could also be harnessed for the conversion of mechanical energy to chemical energy (35). 

Biomedical Applications Due to their excellent blood compatibility (low interaction with plasma proteins) and high oxygen and moisture permeabilities, siloxane containing copolymers and networks have been extensively evaluated and used in the construction of blood contacting devices and contact lenses 376). Depending on the actual use, the desired mechanical properties of these materials are usually achieved by careful design and selection of the organic component in the copolymers. 

Inside the typical smooth muscle cell, the cytoplasmic filaments course around the nuclei filling most of the cytoplasm between the nuclei and the plasma membrane. There are two filamentous systems in the smooth muscle cell which run lengthwise through the cell. The first is the more intensively studied actin-myosin sliding filament system. This is the system to which a consensus of investigators attribute most of the active mechanical properties of smooth muscle. It will be discussed in detail below. The second system is the intermediate filament system which to an unknown degree runs in parallel to the actin-myosin system and whose functional role has not yet been completely agreed upon. The intermediate filaments are so named because their diameters are intermediate between those of myosin and actin. These very stable filaments are functionally associated with various protein cytoarchitectural structures, microtubular systems, and desmosomes. Various proteins may participate in the formation of intermediate filaments, e.g., vimentin. 

The analytic validity of an abstract parallel elastic component rests on an assumption. On the basis of its presumed separate physical basis, it is ordinarily taken that the resistance to stretch present at rest is still there during activation. In short, it is in parallel with the filaments which generate active force. This assumption is especially attractive since the actin-myosin system has no demonstrable resistance to stretch in skeletal muscle. However, one should keep in mind, for example, that in smooth muscle cells there is an intracellular filament system which runs in parallel with the actin-myosin system, the intermediate filament system composed of an entirely different set of proteins, (vimentin, desmin, etc.), whose mechanical properties are essentially unknown. Moreover, as already mentioned, different smooth muscles have different extracellular volumes and different kinds of filaments between the cells. 

Hayash C.I., Shipley N., and Lewis R., Hypotheses that correlate the sequence, structure, and mechanical properties of spider silk proteins, Int. J. Biol. Macromol., 24, 271, 1999. 

Gosline, J.M., Lillie, M., Carrington, E., Gerette, P., Ortleppa, C., and Savage, K., Elastic proteins Biological roles and mechanical properties, Philos. Trans. R. Soc. Land. B Biol. Set, 357, 121-132, 2002. Weis-Fogh, T., A rubber like protein in insect cuticle, J. Exp. Biol., 37, 887-907, 1960. 

As described above, protein domains that provide discrete biological cues (e.g., cell binding) or mechanical properties (e.g., expansion or contraction with temperature changes) can be borrowed from nature and designed into synthetic polypeptides or joined with other polymers to provide bio-inspired function in new... 

Finally, animal, plant and microbial tissues have been shown to contain the iron storage protein ferritin. The animal protein has been extensively studied, but the mechanism of iron binding has not been completely resolved (29). Animal tissues contain, in addition, a type of granule comprised of iron hydroxide, polysaccharide and protein. The latter, called hemosiderin, may represent a depository of excess iron (30). Interestingly, a protein with properties parallel to those of ferritin has been found in a mold. Here the function of the molecule can be examined with the powerful tools of biochemical genetics (31). 

Raw silk was dissolved in hexafluoro-iso-propanol (HFIP) [17, 33]. A typical working concentration for spinning was 2.5% (w/v) silk fibroin in HFIP. The spinning solution was pressed through a small needle (0 80-250 pm) into a precipitation bath (methanol for Bombyx mori silk proteins and acetone for Nephila clavipes silk proteins) and the silk solution immediately precipitated as a fiber. The best performing fibers approached the maximum strength measured for native fibers of Bombyx mori, but did not achieve the mechanical properties of natural spider silk. 

Park SK, Rhee CO, Bae DH and Hettiarachchy NS. 2001. Mechanical properties and water-vapor permeability of soy-protein films affected by calcium salts and glucono-D-lactone. J Agric Food Chem 49(5) 2308-2312. 

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