Instruct offer a wide range of techniques to study macromolecular interactions, including circular dichroism, surface plasmon resonance (SPR), thermal shift assay and calorimetry.
Instruct has 8 centres offering *Macromolecular Interactions across Europe. Navigate the map and click on the pins to discover centres near you.
Instruct offers a large panel of state-of-the-art equipment and expertise in biochemistry and biophysics to perform quality control and functional analysis on protein samples.
Techniques are provided for the biophysical characterization of the structure, function and stability of biological macromolecules like proteins, nucleic acids, lipids and their complexes (Circular Dichroism, Differential Scanning Fluorescence, Differential Scanning Calorimetry, Dynamic Light Scattering, UV/Vis Spectrometry) and kinetic and thermodynamic parameters of their iteration (Microscale Thermophoresis, Surface Plasmon Resonance, Isothermal titration Calorimetry).
Surface Plasmon Resonance (SPR) is a highly sensitive analysis of binding phenomena in real-time without the need for labeling or size limitations
In cellular structural biology the analysis of biomolecular interactions is crucial for describing interaction networks and monitoring multiple complex formation. Surface Plasmon Resonance (SPR) allows a highly sensitive analysis of binding phenomena in real-time without the need for labeling or size limitations. SPR can be used for determining equilibrium constants (Kd), stoichiometry, and association (ka) and dissociation (kd) rates in weak and strong interacting systems, and has applications in molecular assembly, epitope mapping, and small molecule screening. In SPR experiments, one of the interacting moieties is immobilized onto the biosensor surface and the other is free in the solution that is made to flow over the biosensor surface. The response in SPR signal is proportional to the mass of the material bound to the biosensor surface, so large interacting molecules give a more intense signal than small ones. The availability of specific sensor chips for different application purposes makes SPR a powerful tool in structural biology and a basic resource for Instruct.
Thermal shift assay is a thermodenaturation assay to monitor the thermal stability of proteins and investigate factors affecting this stability. This rapid and simple technique is used in high-throughputmode to screen optimalbuffer conditions, ligands, cofactors and drugs for purified proteins. Two methods to monitor protein denaturation are available: a differential scanning fluorimetry (DSF) method and a differential static light scattering method (DSLS). The optimization of proteins solubility and stability properties improvesthe success rate of their structural studies. Changes in the thermal stability of the protein–ligand or protein-peptide complexes relative to the stability of the protein alone allow to rapidly identify promising complexes for further structural characterization and to assign functions.
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