Developing high-throughput MS methods for characterizing structural transitions and stabilities of proteins in solution: From peptides to complexes
Seminar | April 16 | 4-5 p.m. | 120 Latimer Hall
One of the most challenging problems in biochemistry involves understanding how proteins fold. After more than 50 years of work, experimental characterization of protein folding usually leads to results which are described as a cooperative, two phase, transition between the folded and unfolded states i.e., the protein appears to melt. Here we present new data from an IMS-MS analysis of simple proteins that are electrosprayed from a temperature controlled source. The results suggest that the cooperative two state behavior involves other states that are captured in the IMS-MS analysis. In some examples, we find evidence for at least 10 structures that arise at slightly different transition temperatures. The ability to experimentally capture information about new states that are involved in folding and unfolding events may help guide theoretical efforts to model folding processes.
Light refreshments will be served at 3:50 at The Coffee Lab