The research activities within the Division fall mostly within the broad, interdisciplinary field of biophysical chemistry. The ultimate aim is to understand biological systems and processes in terms of the underlying physical and chemical laws. Quantitative studies of biomolecular interactions, dynamics and structure at the molecular level establish the necessary foundation for analyzing higher levels of biological complexity. We also conduct research on liquids, colloids and interfaces, often with a connection to biophysical problems.
Much of our work concerns generic physical properties of proteins in solution: their folding, assembly, aggregation and stability; their three-dimensional structures and conformational dynamics; and their interactions with water, ligands and other biomolecules. We also address more specific, biologically or biomedically inspired, problems from a physico-chemical perspective.
Our principal experimental tool is nuclear magnetic resonance (NMR), in particular nuclear spin relaxation measurements. Our NMR laboratories house seven spectrometers, including state-of-the-art high-resolution instruments, custom-built relaxation dispersion spectrometers and a fast field-cycling instrument. Within CMPS, we have access to a wide range of biophysical techniques, including X-ray crystallography, optical (absorbance, fluorescence, and circular dichroism) spectroscopy, surface plasmon resonance, isothermal titration calorimetry, chromatography and protein engineering. In addition to – and often in close connection with – our experimental studies, we develop NMR theory and methodology. We are also active in analytical and computational modeling of biological and colloidal systems.
For publications and descriptions of current research projects, see the following staff and research group pages:
Much of our research is also documented in PhD theses from the department: