Photoactive yellow protein’s choromophore site, its subsequent structure, and the modification of it.

Abstract

The bacteria genus’s Halobacterium, Ectothiorhodospira, and Rhodobacter possess a unique protein in it that responds to the effects of light absorption, in which the protein will absorb a photon, flex, and then release a photon of its own as the protein changes shape. This unique property can be seen in several different types of proteins spanning several different genera and families of prokaryotes; however it will be specifically the properties of The Photoactive Yellow Protein (PYP) that will be discussed and reviewed in length in this paper. The most common technique that has been used to determine the shape and structure of this protein is most commonly x-ray crystallography. The utilization of this technique provides many unique possibilities as well as challenges, as a generally accepted all-encompassing set of conditions does not exist for proteins; each specific protein of differing amino acid chains will have its own unique set of variables that produce the most effective crystallization. Also, by modifying the presence of an additional and severable tracking and collection mechanism on the protein, these improved isolation abilities allow better purification of the PYP as well as its subsequent encoding genes.