Structural Elucidation of Peptide/Protein Complexes

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Professor Jean Chmielewski, Department of Chemistry, Purdue University is supported by the Organic and Macromolecular Program of the Chemistry Division under a Career Advancement Award to enhance her research expertise in the area structural elucidation using heteronuclear NMR techniques. The interactions leading to the aggregation of five amphiphilic alpha helical peptides, rather the expected four monomeric units, and the unexpected formation of a 1:1 complex between synthetic helical peptide monomers in solution are accessible by heteronuclear NMR. Professor Chmielewski is a highly competent PI, and a sabbatical year spent in the laboratories of investigators at the forefront of protein structure elucidation by heteronuclear NMR will maintain her position at the cutting edge of the protein assembly field. Proteins and peptides are large, flexible molecules whose properties in fluid solution are determined by the molecular structure and aggregation of the monomeric subunits. Heteronuclear NMR offers a means to elucidate the structure of these molecules, and to probe the interactions resulting in aggregation of the monomeric subunits in fluid solution. Professor Chmielewski has embarked on a successful academic career, and expertise in heteronuclear NMR will allow her to continue a very promising research program.