Interaction Direct
This category refers to most frequently used MST applications.
The fluorescence of one molecule is monitored (either intrinsic or dye fluorescence) and the binding is directly detected by a change of thermophoresis of the labeled molecule. The binding is detected even if there is no significant change in molecule mass, size or charge.
Interactions of small fragment–like molecules with a model protein - Carbonic...[more]
AMPA receptors (GluR1–4) are a subtype...[more]
Using MST to analyse the binding of Nanobodies and Nanobody-Fc fusion proteins...[more]
The affinity of a DNA-aptamer to the protein thrombin is measured in different...[more]
Peptide binding to fluorescently labeled protein[more]
Sequence specific small molecule binding to DNA[more]
MST was used to measure the specific interaction of Ca2+-ions...[more]
Label-Free measurement of GPCRs[more]
Binding of a DNA single strand to a labeled double strand[more]
Membrane Vesicle Interaction. MST was used to monitor the docking of two...[more]
measured with fluorescence label and label-free[more]
The binding behaviour of proteins can be easily measured with MST...[more]
AT-hooks are short peptide motifs that bind to the minor groove of AT-rich DNA...[more]
Binding of Small Molecules to labeled p38[more]
Conformational control of protein kinases is an important way of modulating...[more]
The DNA repair protein Ku acts as a heterodimer of Ku70 and Ku80 and binds to...[more]
To understand the interaction of a multimeric ribosomal interactor with the...[more]
Rational Design of Small Molecule Inhibitors Targeting the Rac GTPase-p67phox...[more]
Interaction measured with fluorescence label and label-free. [more]