Biophysical characterisation

Purification and biophysical characterisation of proteins are central steps in structural biology studies. Instruct offers a panel of state-of-the-art equipment and expertise in biochemistry and biophysics to perform quality control and functional analysis on pure protein samples. The biochemical and biophysical characterisation of protein targets are important elements in improving the success rate of their structural studies.

Analytical Ultracentrifugation (AUC)

Study the size and shape of macromolecules in solution to facilitate structural determination of large proteins


Capillary Differential Scanning Calorimeter and Isothermal Titration Calorimeter are instruments generally used in structural biology to charcterize the purified protein samples thermodynamically.

Circular dichroism (CD)

Circular Dichroism

Multi Angle / Dynamic Light Scattering (MALS)

Detailed biophysical characterization of biomolecules in solution

Purification: chromatographic system

Exploit differences in protein properties to isolate a single type of protein from a complex mixture

Purification: Lysis system

Extraction of endogenous or recombinant proteins and protein complexes from cells or tissues and their recovery in solution for further analysis

Surface Plasmon Resonance (SPR)

Highly sensitive analysis of binding phenomena in real-time without the need for labeling or size limitations

Thermal shift assay

Study the thermal stability of proteins and investigate buffer conditions, ligands, cofactors and drugs affecting this stability to rapidly identify promising protein formulation and complexes for further structural characterization