Fluorescence spectroscopy is widely used in biological sciences, biochemistry and biophysics. Intrinsic fluorescence (E.g. tryptophans, tyrosines, phenylalanines, co-factors such as NADH and flavins) as well as site directed fluorescence labeling can be exploited to investigate properties of soluble biological molecules (E.g. proteins, nucleic acids, peptides), membranes and macromolecular complexes in solution.

The spectral characteristics of fluorophors are sensitive to their immediate environment and can be used together with techniques such as fluorescence quenching, resonance energy transfer (FRET) or fluorescence polarization, to study structural changes, dynamics and interactions of macromolecules.

The Shared Instruments Pool depends on acknowledgements to thrive. For more information on how to acknowledge the Shared Instruments Pool and/or its personnel, click here or go to the acknowledgement tab.

Exciting Possibilities in Biology, Biochemistry and Biophysics:

  • Binding curves (ligand - macromolecule, macromolecule – macromolecule, macromolecule - membrane, etc.)
  • Structure and stability of biological macromolecule and complexes
  • Examine conformational changes
  • Distance measurements (FRET)
  • Binding and reaction kinetics
  • And a lot more ...