By Dr C. A. Smith, Dr E. J. Wood (auth.)
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The lone pairs of electrons on the oxygen atoms mean they can attack positvely charged chemical groups, and many enzymes have serine residues that function in catalysis. Often the immediate environment within the protein molecule ensures that a particular serine or threonine residue is especially reactive. Serine and threonine are also common sites for the chemical modifications of proteins. For example, phosphorylation and glycosylation often occur at specific serine or threonine residues. The chemical reagent diisopropylphosphofluoridate reacts irreversibly with some serine residues in proteins.
18. From the properties of biological macromolecules you know about explain why it would not be feasible to use heat to drive metabolic reactions. a / Basic principles 31 7 2 Globular proteins Objectives After reading this chapter you should be able to: D describe the general roles of proteins in biological systems; D explain how the various side groups of amino acids contribute to the structure and functions of proteins; D describe the hierarchial levels of protein structure; D evaluate the importance of forces that determine the structure of a given protein molecule; D illustrate how the biological activities of a selected globular protein may be explained at the molecular level; D explaiIl what is meant by the term protein denaturation.
This feature allows little flexibility and means the polypeptide must adopt a particular shape at sites of proline residues. / 38 Biological molecules L-- / ----' Exercise 2 SERINE and THREONINE both contain alcoholic hydroxyl groups, which can participate in hydrogen bonding. The lone pairs of electrons on the oxygen atoms mean they can attack positvely charged chemical groups, and many enzymes have serine residues that function in catalysis. Often the immediate environment within the protein molecule ensures that a particular serine or threonine residue is especially reactive.