Identification of Differences In Adsorption Between Protein Isoforms

It has been found that an excess or insufficient amount of a specific isoform has the tendency to cause a variety of diseases. Creating a technique to separately identify isoforms will therefore, allow for the prevention of diseases such as various cancers and Alzheimer's. This work tests the difference in adsorption between two monomeric fluorescent protein isoforms. The potential difference in adsorption between the two isoforms will allow one to develop an apparatus to separately identify protein isoforms, based on this difference in adsorption. The fraction adsorbed was used to calculate the percent protein adsorbed for completely folded and partially unfolded protein isoforms. The difference in adsorption ranged from 11 to 53 percent was found in partially denatured proteins. The data has also shown only a slight difference in adsorption when the proteins are in their native states. The type of bead used affected the magnitude and pattern of the adsorption difference between the partially denatured isoforms. The effect of bead surface and protein conformation on adsorption will be discussed.