Branch
Structure & biophysics
4 groups16 techniques16 virtual labs
0 of 16 practised
- Structure determination4 techniques
- X-ray crystallographySolve atomic structures from X-ray diffraction by protein crystals.
- Cryo-EMDetermine 3D structures of large proteins and complexes from frozen particles.
- NMR spectroscopyDetermine structure and dynamics of small proteins in solution.
- Small-angle X-ray scatteringGet the overall size and shape of molecules in solution.
0 of 4 practisedOpen Structure determination → - Folding & stability4 techniques
- Circular dichroismEstimate secondary structure and follow unfolding.
- Thermal shift assaysMeasure protein melting temperature and how much a ligand stabilizes it.
- Differential scanning calorimetryMeasure the heat absorbed as a protein unfolds.
- Intrinsic fluorescenceTrack folding and binding through tryptophan fluorescence.
0 of 4 practisedOpen Folding & stability → - Binding & interactions5 techniques
- Isothermal titration calorimetryMeasure affinity, stoichiometry and binding thermodynamics directly.
- SPR & BLIMeasure real-time binding kinetics to an immobilized partner.
- Microscale thermophoresisMeasure binding in solution using very little sample.
- Fluorescence polarizationDetect a small labelled ligand binding to a larger partner.
- EMSA (gel shift)Show that a protein binds a DNA or RNA probe.
0 of 5 practisedOpen Binding & interactions → - Size & aggregation3 techniques
- Dynamic light scatteringMeasure particle size and detect aggregation in solution.
- SEC-MALSDetermine absolute molecular weight and oligomeric state.
- Analytical ultracentrifugationCharacterize size, shape and complexes by how they sediment.
0 of 3 practisedOpen Size & aggregation →