Analytical & Bioanalytical Techniques

Biography

Biography: Anil K. Shukla

Abstract

Mass spectrometry has become an invaluable tool in proteomics studies with the development of ionization techniques, chromatographic separations and mass spectrometers of higher sensitivity and higher resolution. Majority of these analyses involved digestion of proteins into smaller peptides followed by liquid chromatography separation and mass spectrometry/tandem mass spectrometry analysis. This methodology has proved to be extremely useful in identifying proteins, however, it lacks on correctly identifying post-translational modifications which are very crucial in structure determination and understanding the role played by such modifications. However, tandem mass spectrometry used for identifications of peptides and hence proteins does not always provide necessary information on modification sites and several methods, such as electron capture dissociation and electron transfer dissociation have been developed to obtain better information. It still remains difficult to determine the correct structure of proteins from this information. Top-down proteomics where intact proteins are separated by LC and tandem mass spectrometry is used to fragment these intact protein ions by above techniques to provide a complete description of the primary structure of the proteins and associated modifications. In this presentation, recent developments on the separation and analysis of intact proteins in our lab as well as other labs will be presented.