Abstract
Macromolecules and polymers are the principle building blocks of tissues. Without these large molecules, life as we know it would not be possible, because these moieties are responsible for the completion of most biological processes. Biological macromolecules are classified into four groups of large molecules: proteins, polysaccharides (sugar polymers), nucleic acids, and lipids. These classes are differentiated by their repeat units, the chemical structure that is repeated over and over again to make a large chain. The properties of long chains of repeat units linked together are dependent on the chemistry of the chain. The physical properties of long-chained molecules also depend on the rotational freedom around the backbone, as diagrammed in Figure 2.1. Regardless of the exact chemistry of a macromolecule–s backbone, the physical behavior is fixed. The modulus or resistance of a polymer to deformation is independent of the backbone chemistry, but the temperature at which a particular behavior is observed is dependent on the backbone chemistry. At some temperature, all polymers behave like a rubber band, stretching easily and reversibly. This temperature, at which a polymer behaves like a rubbery material, is the glass-transition temperature. The glass-transition temperature is affected by the chemistry of the repeat unit and by how it affects the backbone flexibility. The relationship between the chemistry of the backbone of a polymer and its rubberiness is more complex than just analysis of the backbone rotational freedom; this is discussed later in this chapter.
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Suggested Reading
Abbas A.K., Lichtman A.H., and Pober, J.S., The Major Histocompatibility Complex, in Cellular and Molecular Immunology, W.B. Saunders Co., Philadelphia, chapter 5, pp. 104–110, 1991.
Atkins E.D.T., Meader D., and Scott J.E., Model for Hyaluronic Acid Incorporating Four Intramolecular Hydrogen Bonds, Int. J. Biol. Macromolec. 2, 318, 1980.
Carlier M.-F., Actin Protein Structure and Filament Dynamics, J. Biol. Chem. 266, 1, 1991.
Furlan M., Structure of Fibrinogen and Fibrin, in Fibrin Stabilization and Fibrinolysis, edited by J.L. Francis, Ellis Harwood Ltd, Chichester, England, chapter 1, pp. 17–64, 1988.
Guido D., Integral Membrane Heparan Sulfate Proteoglycans, FASEB J. 7, 1023, 1993.
Laurent T.C. and Fraser R.E., Hyaluronan, FASEB J. 6, 2397, 1992.
Pauling L. and Corey R.B., The Polypeptide-Chain Conformation in Hemoglobin and Other Globular Proteins, Proc. Natl. Acad. Sci. 37, 282, 1951.
Pauling L. and Corey R.B., Configurations of Polypeptide Chains with Favored Orientations Around Single Bonds: Two New Pleated Sheets, Proc. Natl. Acad. Sci. 37, 729, 1951.
Ramachandran G.N. and Kartha G., Structure of Collagen, Nature 176, 593, 1955.
Ramachandran G.N. and Sasisekharan V., Confomation of Polypeptides and Proteins, Adv. Protein Chem. 23, 283, 1968.
Rayment I. and Holden H.M., The Three-Dimensional Structure of a Molecular Motor, Trends Biochem. Sci., 19, 129, 1994.
Reinhardt D.P., Keene D.R., Corson G.M., Poschl E., Bachinger H.P., Gambee J.E., and Sakai L.Y., Fibrillin-1: Organization in Microfibrils and Structural Properties, J. Molec. Biol. 258, 104, 1996.
Rocco M., Infusini E., Daga M.E., Gogioso L., and Cuniberti C., Models of Fibronectin, EMBO J. 6, 2343, 1987.
Rosenbloom J., Abrams W., and Mecham R. Extracellular Matrix 4: The Elastic Fiber, FASEB J. 7, 1208, 1993.
Rouslahti E., Integrins, J. Clin. Invest. 87, 1, 1991.
Schulz G.E. and Shirmer R.H., Patterns of Folding and Association of Polypeptide Chains, in Principles of Protein Structure, Springer-Verlag, New York, chapter 5, pp. 66–107, 1979.
Scott J.E., Heatley F., and Hull W.E., Secondary Structure of Hyaluronate In Solution: A 1H-N.M.R. Investigation at 300 and 500 MHZ in [2H6] Dimethyl Sulphoxide Solution, Biochem. J. 220, 197, 1984.
Silver F.H., Connective Tissue Structure, in Biological Materials: Structure, Mechanical Properties, and Modeling Soft Tissues, NYU Press, New York, chapter 2, pp. 7–68, 1987.
Smack D.P., Bernhard P.K., and William D.J., Keratin and Keratinization [review], J. Acad. Derm. 30, 85, 1994.
Timpl R. and Brown J.C., The Laminins, Matrix Biol. 14, 275, 1994.
Vincent J.F.V., Proteins, in Structural Biomaterials, Halsted Press, John Wiley and Sons, New York, chapters 2 and 3, pp. 34–83, 1982.
Wertman K.F. and Drubin D.G., Actin Constitution: Guaranteeing the Right To Assemble, Science 258, 759, 1992.
Wilson I.A., Another Twist to MHC-Peptide Recognition, Science 272, 973, 1996.
Yamada K.M., Fibronectin and Other Cell Interactive Glycoproteins, in Cell Biology of Extracellular Matrix, second edition, edited by E.D. Hay, Plenum Press, New York, chapter 4, p. 111, 1991.
Yanagishita M., Function of Proteoglycans in the Extracellular Matrix, Acta Pathol. Jpn. 43, 283, 1993.
Yurchenco P.D., Cheng Y.-S., and Colognato H., Laminin Forms: An Independent Network in Basement Membranes, J. Cell Biol. 117, 1119, 1992.
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Silver, F.H., Christiansen, D.L. (1999). Introduction to Structure and Properties of Biological Tissues. In: Biomaterials Science and Biocompatibility. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-0557-9_2
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DOI: https://doi.org/10.1007/978-1-4612-0557-9_2
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