Structural Elucidation of Peptide/Protein Complexes

Jean Chmielewski教授，普渡大学化学系由化学学部有机和大分子项目支持，并获得职业发展奖，以提高她在使用异核磁共振技术进行结构分析领域的研究专长。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，以及合成的螺旋肽单体在溶液中意外形成的1:1配合物，可以通过异核磁共振得到。Chmielewski教授是一位非常有能力的PI，并且在研究人员的实验室中通过异核磁共振分析蛋白质结构的前沿研究人员度过了一年的休假，这将保持她在蛋白质组装领域的前沿地位。蛋白质和多肽是大而灵活的分子，其在流体溶液中的性质由分子结构和单体亚基的聚集决定。异核磁共振提供了一种手段来阐明这些分子的结构，并探测相互作用，导致聚集的单体亚基在流体溶液中。Chmielewski教授已经开始了成功的学术生涯，在异核磁共振方面的专业知识将使她能够继续一个非常有前途的研究项目。

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.