521-307 Macromolecular Structure, Conformation and Dynamics

Credit Points

Coordinator

Prerequisites

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 and 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.

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; 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%).