Fluorescence and dynamics of structural environment of TRP125 fluorophore in ЕМАР II cytokine
Abstract
The EMAP II cytokine is a multifunctional polypeptide, which reveals dual activities both as a cytokine and a tRNA-binding domain. The intramolecular dynamics of EMAP II cytokine in solution was studied using the methods of fluorescence spectroscopy. The spectrum of tryptophan fluorescence of EMAP II cytokine is caused by the emission of a single Trp125 in protein. The microenvironment of tryptophan residue has been characterized using the fluorescence spectroscopy data and by computer analysis of protein 3D structure. The accessibility of Trp125 in protein globule is about 10%. The rapid conformational dynamics of EMAP II has been revealed using the enhanced quenching of Trp125 fluorescence by acrylamide due to the protein matrix fluctuation in nanosecond time scale.
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