Faculty of Science

Undergraduate - Unit

This unit entry is for students who completed this unit in 2012 only. For students planning to study the unit, please refer to the unit indexes in the the current edition of the Handbook. If you have any queries contact the managing faculty for your course or area of study.

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6 points, SCA Band 0 (NATIONAL PRIORITY), 0.125 EFTSL

Refer to the specific census and withdrawal dates for the semester(s) in which this unit is offered, or view unit timetables.

FacultyFaculty of Science
OfferedGippsland First semester 2012 (Day)
Gippsland First semester 2012 (Off-campus)
Coordinator(s)Dr Walid Daoud


Bioactive chemistry considers naturally occurring compounds and the biosynthetic pathways from which these arise; followed by a study of biological systems used to carry out controlled chemical reactions on organic molecules. The importance of natural product chemistry in relation to biologically active compounds of commercial significance will be illustrated. The course will then focus on concepts of protein chemistry including protein structure, peptide sequencing and synthesis, the principles of folding of polypeptide chains, prediction and modelling of polypeptide structures. The use of proteins as industrial catalysts, in biosensor technology and in immunochemistry will be considered.


On completion of this unit, students will appreciate the range of real world applications for molecules harvested from biological systems; classify a selection of naturally occurring, biologically active molecules into particular classes and outline the general approaches used to isolate, purify and characterise these molecules; describe the general synthetic strategies used by a chemist, utilising both conventional reagents and biological reagents, to design and effect molecular transformations leading to production of medicinal agents; distinguish between primary and secondary metabolites in living systems and describe a selection of biosynthetic pathways including those leading to the formation of natural products of commercial significance; classify selected enzyme controlled reactions, appreciate their role in metabolism and illustrate their applications in biotransformations; describe the experimental strategies for peptide sequencing and the fundamental principles of protein synthesis; describe important aspects of protein architecture; appreciate the fundamental relationship between protein structure and function; compare the properties of biocatalysts and chemical catalysts and consider the industrial applications of biocatalysts; safely perform selected advanced laboratory procedures including: organic synthesis including chemical and enzymatic catalysis; extraction and purification of secondary metabolites from plant material; spectroscopic, electrophoretic and chromatographic analysis; radioimmunoassay and demonstrate advanced level report-writing skills.


Final examination (3 hours) 50%
Assignment: 10%
Problems: 10%
Practical work: 30%

Chief examiner(s)

Associate Professor Jenny Mosse

Contact hours

Three hours of lectures and three hours of laboratory work per week


BTH2752 or CHM2762