The discovery has the potential for revolutionizing the way proteins are assayed in medical, commercial and scientific laboratories which, in turn, could lead to the development of drugs to treat currently incurable diseases. The process, which uses readily available assay materials and techniques, allows for the rapid analyses of large numbers of proteins and gives a visible test result proportionate to the percentage of soluble protein in the sample. As the basic building blocks of cells, soluble proteins act as catalysts and controllers for numerous chemical reactions, in addition to helping give cells, organs and tissues their shape and structure. The range of shapes is governed by interactions among the atoms that make up the protein and the folding process influences functionality. If the protein folds correctly during formation, it will function correctly as a soluble protein.
Misfolded proteins are usually insoluble and useless to a cell.
Since our assay allows researchers to rapidly check proteins for misfolding, this should speed up the development of new assays and drugs to prevent or reverse protein misfolding. Of course, it's not as simple as it sounds, but it's certainly a step in the right direction. The hybrid protein created by this linking has the characteristics of both the GFP and the protein being assayed. If the protein being produced, or expressed, folds correctly then the attached GFP will also fold correctly as it is expressed. If the protein being expressed does not fold correctly, then the GFP will not fold correctly.