521-307 Biomolecular Structure & Bioinformatics

Credit Points

12.5

HECS Band

2

Coordinator

Dr P Gooley

Prerequisites

521-301.

BBiomedSc students: 521-213 and 536-250.

Semester

2 (view timetable)

Contact

Twenty-four lectures (two a week); 36 hours of practicals and workshops

Subject Description

Students will acquire knowledge of the fundamental concepts of determination of protein and nucleic acid structure, and bioinformatics (computational molecular biology) necessary for those who wish to continue studies in relevant areas of structural biology, bioinformatics, protein engineering and rational drug design. Students will also gain an appreciation of the Human Genome Project and its impact on the developing fields of bioinformatics, structural genomics, protein pharmaceuticals and drug discovery.

An overview of the theory and application of methodologies for the determination and computational analyses of macromolecular structures using Nuclear Magnetic Resonance (NMR) spectroscopy, X-ray crystallography, protein molecular dynamics, protein fold recognition, and gene and protein database mining; biophysical methods for investigating macromolecular recognition and interaction.

Subject content includes principles and practice of X-ray crystallography and NMR spectroscopy for determining the three-dimensional structures of biomolecular complexes; the application of X-ray crystallography and nuclear magnetic resonance spectroscopy to structural genomics, rational drug design and screening; use of gene and protein databases to detect biologically significant data; biophysical methods for determining the conformations of proteins and nucleic acids in aqueous solution; molecular dynamics of proteins and the principles of macromolecular recognition including computer-based modelling.

In addition to the specific skills gained through study of this subject, students should develop problem-solving and communication skills in tutorials and report writing.

Assessment

A 2-hour end-of-semester written examination (70%) plus continuous assessment of a laboratory based component (30%).



Status:                   Official 2003
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