Abstract
Fluorescent proteins are the workhorses of biological molecular imaging. Important imaging modalities (such as polarization microscopy or FRET imaging) exploit anisotropic optical properties of fluorescent proteins. The anisotropy (directionality) of optical properties of fluorescent proteins is described by a vector, the transition dipole moment (TDM). Despite the importance of molecular TDM orientation for quantitative structural interpretation of many imaging experiments, experimental data on TDM direction in fluorescent proteins is very limited. Here we present the results of our optical measurements on crystals of representative fluorescent proteins, as well as mathematical interpretation of these results, yielding information on the orientation of TDMs within the investigated fluorescent protein molecules.
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