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Handbook 1997 : Faculty of Science : Biochemistry and Molecular Biology

521-307 Three Dimensional Structure and Conformational Dynamics of Biological Macromolecules

Credit Points:

16.0

Coordinator:

Professor W H Sawyer

Prerequisite/s:

Biochemistry 521-301 (note that 521-203 is strongly recommended) Students should note that the teaching of this subject will assume a sound knowledge of the relevant principles of Chemistry & Physics (to the standard of the prerequisites for 521-203); students who have not completed 521-203 should seek advice from the Department before enrolling in this subject.

Timetable:

Semester 2

Contact:

26 lectures (two a week); 36 hours of practicals and workshops (6 hours every other week)

Objectives:

By the end of the program the student should have acquired:

  • detailed knowledge of the methods used for the determination of three dimensional structures of proteins and nucleic acids by nuclear magnetic resonance spectroscopy and X-ray crystallography;

  • detailed knowledge of spectroscopic methods for investigating the conformations and solution properties of biological macromolecules;

  • an appreciation of the principles of protein molecular dynamics and the application of these principles in the investigation of protein structure and function;

  • knowledge of the theory and practice of experimental approaches to the investigation of intermolecular interactions and macromolecular recognition;

  • advanced practical skills in the use of computers and associated molecular graphics software for the analysis of protein NMR, X-ray crystallography and molecular dynamics data and the modelling of the three dimensional structures of proteins and their ligands.

Content:

Principles and practice of methods for determining the three dimensional structures of proteins and nucleic acids, including X-ray crystallography and nuclear magnetic resonance spectroscopy. Spectroscopic methods for determining the conformations of proteins and nucleic acids in aqueous solution: absorption, fluorescence and circular dichroism spectroscopy. Molecular dynamics of proteins and the principles of macromolecular recognition.

Assessment:

A 2-hour end of semester written examination (70%) plus a computer-based assignment including a written report (30%).

Prescribed Texts:

To be advised at time of enrolment.

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Handbook 1997 : Faculty of Science : Biochemistry and Molecular Biology 
Status:                   OFFICIAL 1997
Last Modified:            Wednesday March 12 3:36 pm
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Copyright © University of Melbourne 1997.