Abstract
Biological materials are extremely well organized in a hierarchical structure from the molecular building blocks at their first level of organization up to the tissue and organ levels with fascinating nonuniform (anisotropic) properties. Nature utilizes hierarchical structures in an intriguing way to self-assemble biomaterials based on molecular building blocks such as amino acids, nucleic acids, polysaccharides, and lipids that are organized into efficient multifunctional structures and systems ranging from the nanoscopic to the macroscopic length scales [1, 2]. The most basic properties and functions of the biomaterials are defined at the very first level of organization. Therefore, it is imperative to incorporate information from the finer scale biological processes, which often govern processes at the coarser scale, to measure the properties and analyze the functions of biological systems.
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References
Alberts, B., Johnson, A., Lewis, J., Raff, M., Roberts, K., & Walter, P. (2002). Molecular Biology of the Cell. New York, Taylor & Francis.
Fratzl, P., & Weinkamer, R. (2007). Nature’s hierarchical materials. Prog. Mater. Sci. 52, 1263–1334.
Gupta, H.S., et al. (2006). Cooperative deformation of mineral and collagen in bone at the nanoscale. Proc. Natl Acad. Sci. USA 103, 17741–17746.
Gupta, H.S., et al. (2007). Evidence for an elementary process in bone plasticity with an activation enthalpy of 1 eV. J. R. Soc. Interf. 4, 277–282.
Buehler, M.J. (2006). Nature designs tough collagen: Explaining the nanostructure of collagen fibrils. Proc. Natl Acad. Sci. USA 103, 12285–12290.
Chan, Hue, & SunDill, K.A. (1993). The protein folding problem. Phys. Today 46( 2), 24.
Chiti, F., & Dobson, C.M. (2006). Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 75, 333–366.
Mesquida, P., Riener, C.K., MacPhee, C.E., & McKendry, R.A. (2007). Morphology and mechanical stability of amyloid-like peptide fibrils. J. Mater. Sci. Mater. Med. 18, 1325–1331.
Iconomidou, V.A., & Hamodrakas, S.J. (2008). Natural protective amyloids. Curr. Protein Pept. Sci. 9, 291–309.
Hardy, J., & Selkoe, D.J. (2002). Medicine: The amyloid hypothesis of Alzheimer’sdisease. Progress and problems on the road to therapeutics. Science 297, 353–356.
Selkoe, D.J. (2001). Alzheimer’s disease: Genes, proteins, and therapy. Physiol. Rev. 81, 741–766.
Tachibana, M., Kobayashi, Y., Shimazu, T., Ataka, M., & Kojima, K. (1999). Growth and mechanical properties of lysozyme crystals. J. Crystal Growth 198, 661–664.
Niemela, P.S., Ollila, S., Hyvonen, M.T., Karttunen, M., & Vattulainen, I. (2007). PLoSComput. Biol. 3, 0304.
Snow, C.D., Sorin, E.J., Rhee, Y.M., & Pande, V.S. (2005). How well can simulation predict protein folding kinetics and thermodynamics? Annu. Rev. Biophys. Biomol. Struct. 34, 43–69.
Cormier, J., Rickman, J. M., Delph, T.J. (2001). Stress calculation in atomistic simulations of perfect and imperfect solids. J. Appl. Phys. 89, 99.
Odegard, G.M., Gates, T.S., Nicholson, L.M., & Wise, K.E. (2002). Equivalent- continuum modeling of nano-structured materials. Comp. Sci. Technol. 6214, 1869–1880.
Zamiri, A., & De, S. (2009). Modeling the mechanical response of tetragonal lysozyme crystals. Langmuir 26(6), 4251–4257.
Harata, K., Muraki, M., & Jigami, Y. (1993). Role of Arg115 in the catalytic action of human lysozyme: X-ray structure of His115 and Glu115 mutants. J. Mol. Biol. 233(3), 524–535.
Tait, S., White, E.T., & Litster, J.D. (2008). Mechanical characterization of protein crystals. Part. Part. Syst. Character. 25(3), 266–276.
Koizumi, H., Tachibana, M., Kawamoto, H., & Kojima\(\dagger \), K. (2004). Temperature dependence of microhardness of tetragonal hen-egg-white lysozyme single crystals. Philos. Mag. 84(28), 2961–2968.
Koizumi, H., Tachibana, M., & Kojima, K. (2006). Observation of all the components of elastic constants using tetragonal hen egg-white lysozyme crystals dehydrated at 42% relative humidity. Phys. Rev. E 73(4), 041910.
Koizumi, H., Kawamoto, H., Tachibana, M., & Kojima, K. (2008). Effect of intracrystalline water on micro-Vickers hardness in tetragonal hen egg-white lysozyme single crystals. J. Phys. D: Appl. Phys. 41(7), 074019.
Koizumi, H., Tachibana, M., & Kojima, K. (2009). Elastic constants in tetragonal hen egg-white lysozyme crystals containing large amount of water. Phys. Rev. E 79(6), 061917.
Alvarado-Contreras, J., Polak, M.A., & Penlidis, A. (2007). Micromechanical approach to modeling damage in crystalline polyethylene. Poly. Eng. Sci. 47(4), 410–420.
Tachibana, M., Koizumi, H., & Kojima, K. (2004). Effect of intracrystalline water on longitudinal sound velocity in tetragonal hen-egg-white lysozyme crystals. Phys. Rev. E 69(5), 051921.
Granato, A.V., Lucke, K., Schlipf, J., & Teutonico, L.J. (1964). Entropy factors for thermally activated unpinning of dislocations. J. Appl. Phys. 35(9), 2732–2745.
Kocks, U.F., Argon, A.S., Ashby, M.F. (1975). Thermodynamics and Kinetics of Slip. In Chalmers, B., Christian, J.W., Massalski, T.B. (Eds.). Progress in Materials Science. New York, Pergamon.
Bunge, H.-J. (1982). Texture Analysis in Materials Science: Mathematical Methods. London, Butterworths.
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De, S., Zamiri, A.R. (2015). Protein Crystals: Molecular to Continuum Level Models Based on Crystal Plasticity Theory. In: De, S., Hwang, W., Kuhl, E. (eds) Multiscale Modeling in Biomechanics and Mechanobiology. Springer, London. https://doi.org/10.1007/978-1-4471-6599-6_2
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