ProtEra provides characterization of target-ligand adducts at different levels of detail. Quick and/or accurate structure of protein-small molecule adducts can be performed. Analysis of the binding affinity through NMR, isothermal calorimetry and fluorimetry are also available.

Determination of binding affinity constants is performed with:
Fluorimetry /Calorimetry (Kd< 10µM)
NMR (Kd from µM to mM)

Structure determination by NMR methods
Characterization of protein-small molecule adducts are provided with the most advanced NMR instrumentation (900 MHz and 800 MHz equipped with cryoprobes, for the highest resolution and sensitivity) by experienced researchers.

Quick structure method (quick but low resolution): - Optimization of sample condition - Backbone resonance assignments - Chemical shift perturbation mapping - Approximate structure calculation Accurate structure method (slow but high resolution): - Optimization of sample condition - Backbone resonance assignments - Side chain resonance assignments - Small molecule assignment - Complete structure determination