fluorescence anisotropy

In chemistry, 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.

Protein structure determination methods
High resolution	X-ray crystallography \| NMR \| Electron crystallography
Medium resolution	Cryo-electron microscopy \| Fiber diffraction \| Mass spectrometry \| SAXS
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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fluorescence anisotropy

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