Oxygen-Binding Function of Microglassified Human Hemoglobin

Jayna Ortenzio
Special Instructions: 
Lunch will be provided between 11:45AM and the beginning of the seminar at noon
Friday, November 11, 2011 - 11:45am
Hudson 125
Seminar Contact(s): 
Chad Gibbs: scg8@duke.edu
Semester & Year: 
Fall 2011
Water is important for activity of proteins in biological systems. It affects protein structure, protein-protein interactions, and protein-ligand interactions. In particular, the hydration of protein surfaces is reflected in the mobility of a protein and in protein folding/unfolding, which in turn affects the protein function. Using human hemoglobin as a model protein, the goal of this research is to ascertain if and to what extent the removal of water of hydration from hemoglobin affects the ability of the protein to reversibly bind oxygen. Hydration is controlled by using a water-competing solvent, such as octanol. The process involves creating a water-in-oil emulsion of the aqueous protein solution as microdroplets dispersed in the water-competing solvent which strips bulk water and water of hydration from the microdroplets to result in a suspension of glassy protein microbeads. The level of protein dehydration depends on the level of water saturation of this competing solvent. Thus, from a materials science perspective, this project examines how a component of the protein composition (waters of hydration), affects secondary and tertiary structures, and how change in structure translates to change in material property of the protein (mobility) which is related to protein function (reversible oxygen-binding).