We've updated our Privacy Policy to make it clearer how we use your personal data.

We use cookies to provide you with a better experience, read our Cookie Policy

Biomolecules: sample and data quality in interaction analysis - two sides of the same coin


Biomolecules: sample and data quality in interaction analysis - two sides of the same coin
Natalia Markova
Principal Scientist - MicroCal and Leader - Scientific Marketing, Bioscience, Malvern Instruments

Dynamic interactions involving biomolecules drive and regulate all biological processes, making interaction analysis a key area of academic and industrial research and development. A variety of biophysical techniques are used in this field, including Nuclear Magnetic Resonance (NMR), Isothermal Titration Calorimetry (ITC), biosensors (such as SPR and BLI) and fluorescence-based assays.

Over the years, clear trends in interaction analysis have driven towards increased ease of use of the advanced techniques, despite the increasing complexity of biomolecules and binding modes being studied.

While methodologies and technologies in interaction analysis continue to evolve, one fundamental prerequisite to the success remains constant: good control over the quality of interacting species, their complexes, and conditions for the binding process. Overlooking this requirement could result in poor performance of a biophysical technique, misleading and irreproducible results and lack of convergence with orthogonal and complementary data generated in a project.

This presentation will give examples which highlight the need for ensuring sample quality and observing good experimental practices for the generation of meaningful and reliable binding data. Case study examples will be given to illustrate the impact of early in-solution profiling of the stability and homogeneity of biomolecules and ligands with:

  • Dynamic Light Scattering (DLS)
  • Differential Scanning Calorimetry (DSC)
  • Multi-Detection Size Exclusion Chromatography (SEC) and
  • Taylor Dispersion Analysis (TDA) 

on the success of research projects in Drug Discovery.


MicroCal range


Isothermal Titration Calorimetry (ITC) 

Dynamic Light Scattering 

Size Exclusion Chromatography (SEC) 

Taylor Dispersion Analysis (TDA) 

Differential Scanning Calorimetry (DSC)



Who should attend? 

Researchers active in Drug Discovery, PIs, Project Leaders, Medicinal Chemists, Structural Biologists, Protein Chemists, Core Facility Managers

What will they learn?

  • Factors impacting the quality of ITC and biosensor data in interaction analysis
  • Ways to improve success rates in interaction analysis
  • Is early profiling of in-solution stability and homogeneity of biomolecules and ligands a waste of time?


Like what you just read? You can find similar content on the communities below.

Cell Science

To personalize the content you see on Technology Networks homepage, Log In or Subscribe for Free