Fluorescence anisotropy
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In biochemistry, fluorescence anisotropy assays the rotational diffusion of a molecule from the decorrelation of polarization in fluorescence, i.e., between the exciting and emitted (fluorescent) photons. This decorrrelation can measure the "tumbling time" of the molecule as a whole, or of a part of the molecule relative to the whole. From the rotational diffusion constants, one can estimate the rough shape of a macromolecule, particularly if it is long and thin.
[edit] See also
| Protein structure determination methods | ||
|---|---|---|
| High resolution: | X-ray crystallography | NMR | Electron crystallography | |
| Medium resolution: | Cryo-electron microscopy | Fiber diffraction | Mass spectrometry | |
| Spectroscopic: | NMR | Circular dichroism | Absorbance | Fluorescence | Fluorescence anisotropy | |
| Translational Diffusion: | Analytical ultracentrifugation | Size exclusion chromatography | Light scattering | NMR | |
| Rotational Diffusion: | Fluorescence anisotropy | Flow birefringence | Dielectric relaxation | NMR | |
| Chemical: | Hydrogen-deuterium exchange | Site-directed mutagenesis | Chemical modification | |
| Thermodynamic: | Equilibrium unfolding | |
| Computational: | Protein structure prediction | Molecular docking | |
| ←Tertiary structure | Quaternary structure→ | |
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