Abstract
Protein splicing is the process by which a polypeptide chain, called an intein, catalyzes its excision from two flanking polypeptides, called exteins, with the exteins ligating together. We are interested in how inteins catalyze the splicing reaction and therefore are studying the mechanism by biophysical means. The lab has studied the third step of protein splicing, asparagine cyclization, via a fluorescence-based assay using a model peptide. Currently, we are analyzing peptide bond cleavage due to cyclization of aspartic acid rather than asparagine, which is promoted at low pH and high temperature. We are currently studying the potential catalytic role of an adjacent histidine residue and carefully determining the influence of pH on the reaction. This material is based upon work supported by the National Science Foundation under grant MCB-1244089 (KVM), The Camille and Henry Dreyfus Foundation (KVM), and Wendell and Kim Weeks (MK).
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