Structural Elucidation of Peptide/Protein Complexes

普渡大学化学系Jean Chmielewski教授获得了化学系有机和高分子项目的支持，并获得了职业发展奖，以增强她在使用异核核磁共振技术进行结构解析方面的研究专长。导致5个两亲性α螺旋肽聚集的相互作用，而不是预期的4个单体单元，以及合成螺旋肽单体在溶液中意外形成1：1复合体的相互作用，可以通过异核核磁共振获得。Chmielewski教授是一位非常称职的PI，在研究人员的实验室里度过了一年的休假时间，她将保持在蛋白质组装领域的前沿地位，这些研究人员处于通过异核核磁共振阐明蛋白质结构的前沿。蛋白质和多肽是大而灵活的分子，其在流体中的性质由单体亚基的分子结构和聚集决定。异核核磁共振为阐明这些分子的结构和探索导致单体亚单位在流体溶液中聚集的相互作用提供了一种手段。Chmielewski教授已经开始了成功的学术生涯，在异核核磁共振方面的专业知识将使她能够继续一项非常有前途的研究计划。

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.