"Nothing tends so much to the advancement of knowledge as the application of a new instrument."

- Sir Humphrey Davy

Research in the Tolley lab is based on the idea that the tools that you have determine the research that you can do. While many areas of research have adequate tools to perform the desired experiments, there are myriad things in studying proteins that are simply not possible to study using existing methods. We develop tools and then perform research that is made possible because of the capabilities of the tools.

One tool developed is dynamic isoelectric focusing (IEF). This is similar to capillary IEF, but it uses additional high voltage power supplies to control the shape of the pH gradient within the capillary. This control permits us to remove focused protein bands without a loss of resolution. Though the actual peak capacity of the system remains unknown, we have shown that it is greater than 1100.

Dynamic IEF is currently being used as a first dimension for proteomic analyses, but it also has great applications in bioassay-guided fractionation (BGF). This is a fancy way of saying that we will separate a sample into fractions and then test them to see which one is biologically active. The unprecedented fractionation capabilities of dynamic IEF open up many areas of research for BGF, including areas such as finding cancer signalling molecules or identifying natural pharmeceutical compounds in plants.

Collaborative research has shown us that there was no good method for finding the protein receptor for a drug or other small molecule. Because of this perceived need, we invented DIABLA. This stands for Dynamic Isoelectric Anisotropy Binding Ligand Assay and combines dynamic IEF and capillary fluorescence anisotropy to discover which proteins bind to a small, fluorescent molecule. DIABLA has many uses, such as screening various tissue samples for unwanted binding or for measuring the binding profile of an individual to customize the dosage of a medicine.