Modeling Intrinsically Disordered Proteins

Chemistry:  Kathryn McMenimen (Mount Holyoke College)
Computer Science: Audrey Lee-St.John (Mount Holyoke College)

Modeling intrinsically disordered proteins

Intrinsically disordered regions of proteins play a large role in protein folding and human diseases. Understanding the movements of these regions could lead to significant advances in predicting folding dynamics and the onset of protein aggregation diseases. Experimental methods are unable to predict the movements of these unstructured regions and reliably determine their range of motions. We propose to use computational techniques to study known intrinsically disordered proteins, incorporating the use of rigidity theory to evaluate the stability and flexibility of their underlying geometric structures. By building a model of the intrinsically disordered regions using standard algorithms from Machine Learning, we expect to be able to gain insight into proteins whose structures are not completely determined. In particular, we plan to investigate the small heat shock proteins currently studied in the McMenimen Lab.