Methods and techniques employed
We use a wide variety of experimental and computational approaches to our address our scientific questions. These include:
Developed over the last century, this technique has allowed us to obtain the 3D structure of proteins and nucleic acids at atomic resolution.
Circular dichroism spectroscopy
This solution technique provides information about protein secondary structure.
We use 2-electrode voltage-clamp methods to measure the functional biophysical properties of ion channels using recombinant DNA technology in frog oocytes.
We use this versatile method for both understanding the structure and function of the proteins we study. Specific approaches include emission, quenching, anisotropy, resonance energy transfer, and time-resolved studies.
Isothermal titration calorimetry enables us to measure the thermodynamic parameters of molecular interactions like the affinity constant, delta G, enthalpy and entropy.
Small angle X-ray scattering
This solution technique allows us to obtain low-resolution structural information including insight into molecular motion.
This solution method allows us to characterise the mass and shape of our macromolecular samples.
Recombinant DNA technology
Molecular biology techniques are used extensively to engineer protein molecules and recombinantly express them in a variety of cell types including bacteria, yeast, and insect cells.
This physical technique allows one to measure absolute molecular mass based on the multi-angle light scattering of the particles, in our case protein complexes.