521-307 3D-Macromolecular Structure and Dynamics

Credit Points

HECS Band

Coordinator

Prerequisites

Biochemistry and molecular biology 521-301 (521-203 is strongly recommended); or 521-213 plus physiology 536-250. Students should note that the teaching of this subject will assume a sound knowledge of the relevant principles of chemistry 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.

Semester

Contact

Subject Description

By the end of the subject the student should understand the methods used for the determination of three-dimensional structures of proteins and nucleic acids by nuclear magnetic resonance (NMR) and X-ray crystallography; spectroscopic methods for investigating the conformations and solution properties of biological macromolecules; the principles of protein molecular dynamics and their applications in investigations of protein structure and function; the theory and practice of experimental investigations of macromolecular recognition and other interactions; and advanced practical skills in computational analysis of protein NMR, X-ray crystallography and molecular dynamics data and the molecular modelling of the structures of proteins and their ligands. Subject content includes 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 including computer-based modelling.

Assessment

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