All biological processes involving biochemical reactions and relationships which are dependent on structure-function are driven or limited by intermolecular interactions. Researchers working within drug discovery for both small and large molecules have a primary requirement to understand the interactions of their candidate molecules with drug target protein molecules. The binding of two molecules, both in terms of strength and stoichiometry, provides a wealth of information which can help direct the rank-ordering of candidates.

The way in which two molecules interact with one another can be simple and straightforward, or may be much more complex - affected by other intermolecular interactions such as hydrogen bonding, hydrophobic and Van der Waals forces, and electrostatic interactions. Ideal for monitoring binding interactions are label-free, tag-free, direct measurement techniques which produce reliable, high-quality data, even for complex interactions. 

Malvern Panalytical provides label-free, gold standard technology to act as a universal tool for studying both small molecule:protein and protein:protein interactions: 

Biomolecular interactions

  • Thermodynamic characterization of the relationship between two molecules

Enzyme kinetics

  • Understanding and characterizing enzymatic reactions, to assist with research into disease pathways, drug discovery and the development of biofuels

MicroCal ITC Linie

MicroCal ITC Linie

Bestimmung der Bindungsparameter von Biomolekülen in einer einzigen Analyse

Mehr Details
Typ der Messung
Markierungsfreie Analyse
Temperaturbereich 2°C - 80°C
Probendurchsatz x per 24h day - 42per 24h day
Technologie
Mikrokalorimetrie
Isothermale Titrationskalorimetrie (ITC)