10.0 Associate Professor G J Howlett Biochemistry and Molecular Biology 521-201 and 521-202 or 521-203, or Biological Chemistry 521-024. First semester 26 lectures (two a week) By the end of the program the student should have acquired:

• An understanding of the general properties of proteins which determine the relationships between protein structure, function and stability;
• An understanding of how protein design and engineering can be used for investigating structure-function relationships;
• A theoretical background to the major techniques used in modern protein chemistry and an appreciation of their applications in biotechnology.

Separative and analytical techniques in protein chemistry. Evolution of sequence and function. Structure and function of immunoglobulins, T cell receptors and antigen presentation. Vaccines, monoclonal and recombinant antibodies and immunodiagnostic applications. Protein design and engineering; chemical synthesis of engineered proteins; the importance of molecular graphics; effects of point mutations on tertiary structure and biological function; protein design for biotechnology, with major examples including enzymes and immunological reagents particularly chimaeric antibodies and immunotoxins. Analysis of protein conformation; determinants of protein folding; sequence algorithms for structural prediction, circular dichroism, fluorescence and difference spectroscopy, nuclear magnetic resonance. Analytical and preparative ultracentrifugation. Binding of small molecular weight molecules to proteins and drug design; cooperative interactions and their significance. Protein-protein and protein-DNA interactions. Enzymes: reaction kinetics, one and two substrate reactions, multienzyme complexes, genetically engineered enzymes, immobilised enzymes and their applications in industry. A 2-hour end-of-semester written examination. Branden C and Tooze J Introduction to Protein Structure 1991 Garland 8 Assoc. Prof. G J Howett 521-024 Biological Chemistry First semester 26 hours of lectures.