Elasticity proteins

Maruyama, 1997] Maruyama, K. Connectin/titin, a giant elastic protein of muscle. FASEB J. 11 (1997) 341-345... 

Two cytoskeletal proteins, tltln (also known as connectm) and nebulm, account for 15% of the total protein in the myofibril. Together these proteins form a flexible filamentous network that surrounds the myofibrils. Titin is an elastic protein and can stretch under tension. Its discovery and characteriza-... 

FIGURE 17.21 A drawing of the arrangement of the elastic protein titin in the skeletal mnscle sarcomere. Titin filaments originate at the periphery of the M band and extend along the myosin filaments to the Z lines. These titin filaments produce the passive tension existing in myofibrils that have been stretched so that the thick and thin filaments no longer overlap and cannot interact. (Adapted from Ohtsuki, ., Maruyama, K, and Ebashi,. S ., 1986. Advances ia Protein Chemisti y 38 1—67.)... 

Fumaric acid breaks the sulfur-to-sulfur bonds in the elastic protein gluten in bread doughs. This makes the doughs more machine-able. It also is a key ingredient in rye and sourdough breads—it makes them sourer. 

All elastic proteins contain distinct domains, of which at least one is made up of elastic repeat sequences, and they all contain cross-links between residues in either the nonelastic or elastic domains [9]. Previously, the Drosophila CGI5920 gene was tentatively identified as one encoding a resUin-like protein [31]. To prepare recombinant resilin, we chose to express the first exon of the Drosophila CG15920 gene [29], which encodes an N-terminal domain in the native protein comprising 17 copies of the putative elastic repeat motif GGRPSDSYGAPGGGN [31]. 

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. 

DW Urry, A Pattanaik. Elastic protein-based materials in tissue reconstruction. Ann NY Acad Sci 831 32-46, 1997. 

Maruyama, K. (1976). Connectin, an elastic protein from myofibrils. / Biochem. (Tokyo) 80, 405-407. 

The protein elastin presents another opportunity to create amyloid-like fibrils from natural proteins for the purpose of developing biomaterials. Elastin is found in tissue where it imparts elastic recoil, and fibrils formed from this protein may demonstrate some of the elastic properties of the constituent elastic proteins (Bochicchio et al., 2007). Elastin typically contains the sequence poly(ZaaGlyGlyYaaGly) (where Zaa, Yaa = Val or Leu) (Tamburro et al., 2005), and short stretches of the protein retain the ability to form structures similar to the original protein. Simple proline to glycine mutations in the hydrophobic domains of elastin can induce the formation of amyloid-like fibrils (Miao et al., 2003), suggesting that fibrillar materials can be easily generated from these sequences. 

Proteolytic enzymes (proteases) are involved in a wide variety of physiological processes including digestion, fertilization, coagulation, and the immune response. Outside of their normal environment, proteases can be extremely destructive and natural human plasma inhibitors inhibit most proteases that escape. Imbalance in protease-protease inhibitor systems can lead to a number of diseases of which pulmonary emphysema is one well-characterized example. This disease results when the protease elastase attacks elas-tin, the major elastic protein in the lung. Considerable effort has been devoted to the synthesis of inhibitors of proteolytic enzymes such as elastase for possible therapeutic use. In the future, specific and selective synthetic protease inhibitors should be useful for treating specific diseases that range from the common cold to chronic disorders such as emphysema. 

Shewry, P., Halford, N., Belton, P., and Tatham, A. (2002). The structure and properties of gluten An elastic protein from wheat grain. Phil. Trans. R. Soc. Land. B 357,133-142. 

The gas bubbles in food foams are separated by sheets of the continuous phase, composed of two films of proteins adsorbed on the interface between a pair of gas bubbles, with a thin layer of liquid in between. The volume of the gas bubbles may make up 99% of the total foam volume. The contents of protein in foamed products are 0.1-10% and of the order of 1 mg/m2 interface. The system is stabilized by lowering the gas-liquid interfacial tension and formation of rupture-resistant, elastic protein film surrounding the bubbles, as well as by the viscosity of the liquid phase. The foams, if not fixed by heat setting of the protein network, may be destabilized by drainage of the liquid from the intersheet space, due to gravity, pressure, or evaporation, by diffusion of the gas from the smaller to the larger bubbles, or by coalescence of the bubbles resulting from rupture of the protein films. 

The amino group of lysine is the second protein side chain frequently applied by nature for the cross-linking of proteins. In elastin, the elastic protein of... 

Urry DW. Physical chemistry of biological free energy transduction as demonstrated by elastic protein-based polymers. J Phys Chem B 1997 101 11007-11028. 

Elastin A very elastic protein found in blood vessels. 

Table 1. Hydrophobicity scale for protein-based polymers and proteins based on the properties of the inverse temperature transition of elastic protein-based polymers, poly[/v(GVGVP), (GXGVP)]. ...

In contrast, other elastic proteins show precisely the opposite property, i.e., they dissipate a negligible amoimt of energy in a stress-strain cycle or, equiv-... 

Therefore, TMDSC has been demonstrated to be an effective method to split the overlapping phenomena present in the ITT of elastic protein-based polymers. By tuning the frequency of the periodic component, a maximum split can be achieved that shows an exothermic contribution arising from the Van der Waals contacts attending chain folding and assembly, and an endothermic contribution associated with loss of hydrophobic hydration, the... 

Lee J, Macosko CW, Urry DW (2001) J Biomater Sci Polym Edn 12 229 Nicol A, Gowda DC, Parker TM, Urry DW (1993) J Biomed Mater Res 27 801 Urry DW (2003) Elastic protein-based biomaterials elements of basic science, controlled release and bio compatibility. In Wise DL, Hasirci V, Yaszemski MJ, Alto-belli DE, Lewandrowski KU, Trantolo DJ (eds) Biomaterials handbook-advanced applications of basic sciences and bioengineering. Marcel Dekker, New York Meyer DE, Kong GA, Dewhirst MW, Zalutsky MR, Chilkoti A (2001) Cancer Res 61 1548... 

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