BIOPHYSICS BIOCHEMISTRY

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

SPR Request Form MST Request Form

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Biophysical and Biochemical Platforms

Biophysics Biochemistry

Binding

MST, SPR, nanoDSF, DSF, ITC, HTRF, TR-FRET, FP, SwitchSense, Mass spectrometry, 1H and 19F NMR

STD (Saturation-Transfer Difference) NMR

nanoDSF
(differential scanning fluorometry)

MST
(MicroScale Thermophoresis)

Kinetics

SPR, HTRF, TR-FRET, SwitchSense

SwitchSense

SPR (Surface plasmon resonance)

Thermodynamics&Stoichiometry

ITC, SPR, MST &SPR, ITC, MST

Function

HTRF, TR-FRET, SwitchSense, various biochemical assays (luminescence, fluorescence, colorimetric read-out)

SwitchSense

SPR (Surface plasmon resonance)

Protein Quality

nanoDSF, DSF, DLS, Mass spectrometry

Bodipy-GTP nucleotide exchange assay

LC-MS

Complete biophysical characterization of your compound series

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 uM
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-100uM
Dynamic Light Scattering (DLS)	Measures particle assize across the range ~0.1 nm to 10 um Low probe consumption	Low resolution Large particles even when present in small quantities may impact the measurement	Translational diffusion coefficient (D_t), R_h, d_h, B₂₂, k_D, viscosity
Fluorescence Polarization (FP)	Homogenous assay	Narrow measurement window Sensitive to fluorescence interference	K_d 1nM - 1mM
Homogeneous Time Resolved Fluorescence (HTRF)	Homogenous assay Highly sensitive and robust	Requires two labels	K_d, EC₅₀, k_on, k_off 1pM - 1mM
Isothermal Titration Calorimetry (ITC)	Direct determination of thermodynamic parameters for a binding event	Very high protein consumption Requires high solubility of titrated component	K_d, ΔH, ΔS, ΔG, stoichiometry 1nM - 100μM
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	K_d 1pM - 1mM
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	T_m, C_m, &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	k_on, k_off, stoichiometry 1pM - 500μM
SwitchSense	Molecular dynamics Conformational change	Immobilization to DNA required	k_on, k_off, K_d, d_h, stoichiometry
Time-Resolved Fluorescence (TR-FRET)	Homogenous assay Highly sensitive and robust	Requires two labels	K_d, EC₅₀, k_on, k_off 1pM - 1mM

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