Fluorescence Spectroscopy And The Emission Wavelength Of Eosin Serum Albumin ( Bsa )

1141 Words May 5th, 2016 5 Pages
Abstract Fluorescent properties are used to study protein and small molecule interactions. Fluorescent spectrophotometry determined the excitation wavelength of eosin isothiocyanate to be 525 nm and its emission wavelength was 545 nm. Glycogen phosphorylase was similarly studied. The excitation wavelength was 330 nm and the emission wavelength was 360 nm. The emission wavelength could be indicative of the presence of the fluorophore, tryptophan. The potential interaction between bovine serum albumin (BSA) and 1-anilino-8-naphthalene sulfonic acid (ANS) was studied through fluorescence and fluorescence resonance energy transfer (FRET). BSA had an emission wavelength of 358 nm which could also be indicative of a tryptophan. When BSA and ANS were mixed together, the emission wavelength was longer suggesting that the molecules interact with each other and follow FRET.
Fluorescence spectroscopy is a useful technique to determine the proteins and nucleic acids of a macromolecule. Some molecules, fluorophores, can absorb light at certain wavelengths and then emit it at another wavelength. When the molecule absorbs light it is excitation and the light released is emission. The light particles, photons, hit a fluorophore to excite the molecule (Voet et. al 2013). Excitation occurs by the valence electrons of the molecule receiving energy and moving to a higher energy state from the ground state. The excited electrons will later return to the ground state because they…
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