Our ligand binding capabilities leverage both ligand-observed and target-observed NMR methods, enabling the identification of small-molecule binders, as well as protein–protein, nucleic acid, and peptide–target interactions. A key advantage of NMR-based ligand binding studies is that experiments are performed under physiologically relevant conditions, ensuring results that closely reflect true biological behavior.

​

​

 

​

​

​

​​​

Ligand-Observe Methods (e.g. STD/ waterLOGSY/ CPMG)

​

​These experiments focus on the spectral properties of the ligand, are not limited by target size and can provide the following information:

​

• Provide rapid turnaround with high sensitivity

• Require only small amounts of target and compound

• Deliver a clear yes/no assessment of ligand binding

• Offer insights into the nature of ligand–target interactions

• Determine ligand binding stoichiometry

​

Target Observe Methods (e.g. HSQC/HMQC)​​​​

​

These experiments focus on the spectral properties of the target and provide powerful insights into:

​

• Provide powerful insights into ligand binding site location

• Reveal conformational changes in the target upon ligand binding

• Deliver mechanistic understanding that can serve as a cornerstone for the chemistry/biology in therapeutic programs

• Typically require 2D NMR methods and an isotopically labeled target

​

Binding constant determination (Kd)

​

Both ligand and target observe experiments can be used to accurately and precisely measure the affinity (dissociation constant, Kd) of ligands to their targets under biologically relevant conditions.

​

​