Ion mobility mass spectrometry (IMMS) is a powerful analytical technique that is increasingly being used in the field of structural biology. Ion mobility separates ions according to shape and allows the study of conformational changes in biological systems that are not amenable to analysis by more established biophysical methods. When coupled to mass spectrometry, ion mobility allows one to distinguish between co-existing forms of a protein, which cannot easily be achieved by other approaches.
The development of new technologies and methods necessitates the concurrent development of computational methods and software to process the data. We have been developing method to process mass spectrometry data and have developed the first open source software for the processing of travelling wave ion mobility mass spectrometry data. For more information and to download our code please visit the resouces page.
The way proteins fold is of paramount importance. A number of diseases are the result of protein misfolding and subsequent aggregation. The list of these diseases include Alzheimer’s, Prion diseases, etc. In our lab we are interested in alpha 1-antitrypsin (A1AT), which is the archetype of the serpin (serine protease inhibitor) superfamily of proteins. It is predominantly synthesized in hepatocytes and secreted into the circulation at the highest levels of any serum antiprotease. Under physiological conditions it protects the lungs from human neurophil elastase but upon aggregation it is implicated in chirosis of the liver and chronic obstructive pulmonary disease.