Methods and techniques employed

 

We use a wide variety of experimental and computational approaches to our address our scientific questions. These include:

X-ray crystallography

X-ray crystallography

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

Circular dichroism spectroscopy

This solution technique provides information about protein secondary structure.

Voltage-clamp electrophysiology

Voltage-clamp electrophysiology

We use 2-electrode voltage-clamp methods to measure the functional biophysical properties of ion channels using recombinant DNA technology in frog oocytes.

Fluorescence spectroscopy

Fluorescence spectroscopy

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.

Calorimetry

Calorimetry

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

Small angle X-ray scattering

This solution technique allows us to obtain low-resolution structural information including insight into molecular motion.

Analytical ultracentrifugation

Analytical ultracentrifugation

This solution method allows us to characterise the mass and shape of our macromolecular samples.

Recombinant DNA technology

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.

Light scattering

Light scattering

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.

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