Systematic organization of protein complexes as well as protein-directed formation of inorganic solids enables living organisms to achieve a high density of functionality and create hierarchical materials with unique properties. Conversely, when these processes proceed without the proper level of control, they often result in disease. Consequently, developing a fundamental understanding of the thermodynamic and kinetic controls on protein and protein-directed assembly can define new strategies towards both materials synthesis and the treatment of disease.

Modern molecular imaging methods, such as optical imaging and magnetic resonance, are commonly limited by the amount of molecule-specific contrast they generate. Most MR images simply show water; most interesting endogenous targets for optical imaging do not fluoresce, hence they can only be detected by absorption methods that are limited by scattering. I will review two recent developments-intermolecular multiple-quantum MR imaging, and nonlinear optical imaging using femtosecond pulse shaping-which use new physics to increase the range of applicability of these techniques.