The central idea of this course is free energy, the quantitative way we understand thermodynamic forces driving the equilibria and transition rates in chemistry, physics and biology. We describe the components underpinning free energy: entropy and internal energy. We explore the microscopic interactions - including hydrogen bonding, van der Waals interactions, electrostatics and hydrophobic forces - that explain physical and chemical mechanisms in cell biology and are the workhorse tools in computational drug discovery. We show how these basic ideas are applied: binding affinities form the basis for synthetic biology and drug discovery; coupled binding explains how biological machines convert energy and transduce signals or control gene activity; and polymer free energies form the basis for the folding of protein and RNA molecules; with implications for molecular and cellular evolution.
Textbooks:
Molecular Driving Forces, by Dill, Bromberg, Kocher & Balázsi. 3rd Ed. MIT Press, 2026
Protein Actions by Bahar, Jernigan & Dill. Garland Science, 2017
Extra textbook: Physical Models of Living Systems by Nelson. W. H. Freeman & Co., 2015