Course Outline

Introduction to protein structure and function

Biological systems and biomolecules, nucleic acids and proteins, protein structure, fibrous proteins, globular proteins, X-ray diffraction from protein crystals, electron density maps, protein function.

Stereochemistry of Proteins

Linear polymers, random walk model of linear polymers, elasticity of polymers, proteins as polymers, the peptide bond, steric hindrance, side chian properties, van der Waals interactions, Lennard-Jones (6-12) potential, electrostatic interactions, hydrogen bonds.

Protein thermodynamics (how do proteins fold?)

Free energy and entropic forces, solvent interactions and solvent entropy, polypeptide chains in water, the folding process, folding pathways, simulations and predictions, experimental studies on folding, rapid laser heating of proteins, effects of mutation on folding rates, relative contact order, transition states.

Protein dynamics (how do proteins function?)

Excitement and relaxation of protein structure, equilibrium fluctuations, kinetics of proteins, proteins as complex systems, multiple conformational states of native proteins, protein function, functionally important motions.

Unfolding single protein molecules

Atomic force microscopy, force spectroscopy, the worm-like chain model for biopolymers.

Resources

Assignments, Lecture Notes and Past exams

Links

UWA Biophysics Homepage

Lecturer