Biophysics & Biochemistry

Very diverse technology platform facilitates target validation, enables fast hit finding, hit confirmation, and supports lead series optimization.


The broadest technology suite for hit-finding & confirmation accessible


Binding
MST, SPR, nanoDSF, DSF, ITC, HTRF, TR-FRET, FP, SwitchSense, Mass spectrometry, 1H and 19F NMR
Kinetics
SPR, HTRF, TR-FRET, SwitchSense
Thermodynamics
ITC, SPR, MST
Stoichiometry
SPR, ITC, MST
Function
HTRF, TR-FRET, SwitchSense, various biochemical assays (luminescence, fluorescence, colorimetric read-out)
Protein Quality
nanoDSF, DSF, DLS, Mass spectrometry



Complete biophysical characterization

Complete biophysical characterization of your compound series


Download more information (Biophysics & Biochemistry)

Comparison of methods



Advantages Disadvantages Information obtained and Range
Affinity Selection Mass Spectrometry (AS-MS)
  • High-throughput
  • Can be applied to solubilized membrane proteins
  • Ligand mass detection allows verification of compound structure
  • Low-affinity binders are hard to detect
< 10 µM
Differential Scanning Fluorimetry (DSF)
  • Estimates the effect of the ligand on the thermal stability of a protein
  • Fast and robust assay development
  • Requires a fluorescent dye
  • Artefacts occur owing to fluorescence quenching or aggregation
1 nM–100μM
Dynamic Light Scattering (DLS)
  • Measures particle assize across the range ˜ 0.1 nm to 10 µm
  • Low probe consumption
  • Low resolution
  • Large particles even when present in small quantities may impact the measurement
Translational diffusion coefficient
(Dt), Rh, dh, B22, kD, viscosity
Fluorescence Polarization (FP)
  • Homogenous assay
  • Narrow measurement window
  • Sensitive to fluorescence interference
Kd
1 nM – 1 mM
Homogeneous Time Resolved Fluorescence (HTRF)
  • Homogenous assay
  • Highly sensitive and robust
  • Requires two labels
Kd, EC50, kon, koff
1 pM – 1 mM
Isothermal Titration Calorimetry (ITC)
  • Direct determination of thermodynamic parameters for a binding event
  • Very high protein consumption
  • Requires high solubility of titrated component
Kd, ΔH, ΔS, ΔG, stoichiometry
1 nM – 100 µM
Microscale Thermophoresis (MST)
  • In-solution measurements
  • Applicable also for challenging targets (e.g., IDPs, solubilized membrane proteins)
  • Low probe consumption
  • Requires labeling of the target with a fluorophore or strong intrinsic fluorescence
  • Low protein consumption
Kd
1 pM – 1 mM
Nano-Differential Scanning Fluorimetry (nanoDSF)
  • Estimates the effect of the ligand on the thermal stability of a protein
  • Fast and robust assay development
  • Relies on intrinsic fluorescence of a protein
  • Low protein consumption
  • No measurements possible when protein lacks tryptophan or tyrosine residues
Tm, Cm, &DeltaG
Surface Plasmon Resonance (SPR)
  • Time-resolved quantification of interactions
  • Requires immobilization of the probe to the surface
  • Requires highly stable protein
  • Signals affected by solvent effect
kon, koff, stoichiometry
1 pM – 500 µM
SwitchSense
  • Molecular dynamics
  • Conformational change
  • Immobilization to DNA required
kon, koff, Kd, dh, stoichiometry
Time-Resolved Fluorescence (TR-FRET)
  • Homogenous assay
  • Highly sensitive and robust
  • Requires two labels
Kd, EC50, kon, koff
1 pM – 1 mM



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