Handbook 1996 : Faculty of Science (Volume 4 page 171)
Biochemistry subject : Next:521-302 | Prev:521-203 | Search | Help
521-301 "Protein Structure, Design and Engineering" appears differently in several places - choose the one you want:
1. Biochemistry, Faculty of Science (v4, p171) : Next:521-302 | Prev:521-203
Credit points: 10.0
Coordinator: Associate Professor G J Howlett
Prerequisite: Biochemistry and Molecular Biology 521-201 and 521-202 or 521-203, or Biological Chemistry 521-024.
Contact: 26 lectures (two a week)
Timetable: First semester
Objectives:
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.
Content:
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.
Assessment:
A 2-hour end-of-semester written examination.
Prescribed texts:
1. Biochemistry, Faculty of Science (v4, p171) : Next:521-302 | Prev:521-203
2. Agriculture, Faculty of Agric, For & Hort (v4, p18) : Next:521-302 | Prev:212-413
Year 4 Agriculture.
Credit points: 8
Coordinator: Assoc. Prof. G J Howett
Prerequisite: 521-024 Biological Chemistry
Contact: 26 hours of lectures.
Timetable: First semester
See additional details under the Biochemistry subject above.
* Note that CONTACT, COORDINATOR, POINTS, PREREQUISITES differs from the maintainer's version above. A log of variations is available.
2. Agriculture, Faculty of Agric, For & Hort (v4, p18) : Next:521-302 | Prev:212-413
Status: Official 1996 Date created: Oct 9 1995 Last modified: Oct 9 1995 Authorised by: Academic Registrar Email enquiries: Course_Information@registrar.unimelb.edu.au
Maintained by: Dept. of Biochemistry & Molecul.Biology, Faculty of Medicine, Dentistry and Health Sciences.
Copyright © University of Melbourne 1995,1996.