Gas Phase Proteins

Proteins are key to living systems; they store and transport the molecules essential to life. At the molecular level, proteins and peptides are linear polymers of twenty common amino acids. Unlike other polymers, proteins and larger peptides are remarkable in that the linear chain very rapidly adopts a unique three-dimensional conformation in the aqueous (water) environment in which it is found. Interactions of proteins with water are expected to play a significant role in protein folding into a three-dimensional structure; however these interactions and the role they play in three-dimensional structure are still not well understood. In this talk, we will explore the structure of proteins and the effect of removing the proteins from the water and studying them in the gas phase. We will discuss recent research conducted by Grinnell students focused on characterizing the structure(s) of small peptides in the gas phase and our efforts to understand the role water plays in determining protein struc ture

Elaine Marzluff, associate professor of Chemistry, earned her A.B. (with high honors in Chemistry) from Harvard University and her Ph.D. in Chemistry from the California Institute of Technology. Professor Marzluff is interested in the structure and dissociation mechanisms and energetics of peptides and proteins in the gas phase. She couples electrospray ion trap mass spectrometry with collisional activated dissociation and Hydrogen Deuterium exchange reactions to probe the gas phase structure of biological molecules. Her research also focuses on the fundamental issues associated with the activation and dissociation dynamics of large molecules in the gas phase.