With the support of the Organic Dynamics Program in the Chemistry Division, Professor Richard P. Cheng of the Chemistry Department at the State University of New York at Buffalo (SUNY-Buffalo) will perform research that will serve as a first step towards understanding the effect of side chain length of charged amino acids on protein electrostatic interactions, which are important for stabilizing protein structures, and for protein-protein and protein-ligand recognition. The proposed studies will provide insight into why nature incorporates charged amino acids with varying side chain lengths, electrostatic interactions with phosphoserine, and effects of the helix dipole on intrahelical ion pairs. These studies will also lay the foundation for utilizing charged functionalities with various linker lengths in designing peptides, molecules, and materials for applications in biotechnology.
This research by Professor Cheng of SUNY at Buffalo on the effect of side chain length on intrahelical electrostatic interactions will provide excellent training for graduates and undergraduates. Research in Professor Cheng?s lab will enable students to integrate multiple techniques including organic synthesis, solid phase peptide synthesis, and statistical mechanical and conformational analysis. The collaborations in the proposed research will provide students the opportunity to interact with other scientists. The results of the research will be presented at professional meetings and published in peer-reviewed scientific journals. Professor Cheng also proposes to produce and podcast interviews (by students) with scientists on recent publications in protein and peptide research. The students will be exposed to the current frontier of protein and peptide research by interviewing leading scientists and formulating in depth questions. The podcasts will target the general public and students with the goal of distributing recent scientific findings, educating the general public, and recruiting future scientists.
