Proteins

  • John M. deMan
Part of the Food Science Text Series book series (FSTS)

Abstract

Proteins are polymers of some 21 different amino acids joined together by peptide bonds. Because of the variety of side chains that occur when these amino acids are linked together, the different proteins may have different chemical properties and widely different secondary and tertiary structures. The various amino acids joined in a peptide chain are shown in Figure 3-1. The amino acids are grouped on the basis of the chemical nature of the side chains (Krull and Wall 1969). The side chains may be polar or non- polar. High levels of polar amino acid residues in a protein increase water solubility. The most polar side chains are those of the basic and acidic amino acids. These amino acids are present at high levels in the soluble albumins and globulins. In contrast, the wheat proteins, gliadin and glutenin, have low levels of polar side chains and are quite insoluble in water. The acidic amino acids may also be present in proteins in the form of their amides, glutamine and asparagine. This increases the nitrogen content of the protein. Hydroxyl groups in the side chains may become involved in ester linkages with phosphoric acid and phosphates. Sulfur amino acids may form disulfide cross-links between neighboring peptide chains or between different parts of the same chain. Proline and hydroxyproline impose significant structural limitations on the geometry of the peptide chain.

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Copyright information

© Springer Science+Business Media New York 1999

Authors and Affiliations

  • John M. deMan
    • 1
  1. 1.Department of Food ScienceUniversity of GuelphGuelphCanada

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