EAGER: Elucidating Protein - Colloid Interactions for Enhanced Bio-Energy Applications

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PI: Somasundaran, PonisserilProposal Number: 1242524Institution: Columbia UniversityTitle: EAGER: Elucidating Protein - Colloid Interactions for Enhanced Bio-Energy ApplicationsAn emerging trend in alternative energy technologies is the use of enzymes or other functional proteins to generate energy; this can already be seen in bio-fuel efforts, where enzymes are used to break down crystalline cellulose into simpler sugars. More radical approaches to ?bio-energy? include bio-fuel cells, where enzymes are the catalysts that oxidize sugar to generate a current; or bio-solar which takes advantage of photosynthetic proteins to capture and harness photonic energy. The ecological advantages are apparent: enzyme catalyzed processes are low temperature and require no harsh solvents. However, the challenge lies in finding ways of maximizing their stability and function outside of a biological environment.The goal of this EAGER project is to explore the unknown interactions that arise from protein ? colloid interactions; specifically those that enable active portions to seemingly ?perceive? their environment through the protein structure in which they are embedded. Whatever mechanisms responsible for these macromolecular sensory phenomena may be responsible for the synergistic interactions which occur between non-ionic surfactants and enzymes, resulting in increased enzyme activity.PI hypothesizes that surfactant aggregates (micelles) interact with the external structure of enzymes to affect changes in fluctuations, causing sub-angstrom scale dynamic motions which ultimately affect the active site position and range of motion. The PI will study this novel concept through a exploratory research plan - starting with a foundation in comparing enzyme kinetics, to understanding colloid and protein structure behavior, and then molecular dynamic modeling. From these observations, the PI intend to develop a thorough model of the physical interactions that occur between the enzyme structure and surfactants as well as surfactant-aggregates, with the ultimate goal of determining if there is a connection between non-ionic surfactant micelles, enzyme structure flexibility and enzyme activity.This previously unexplored concept attempts to build a bridge between the bulk interactions of enzyme kinetics in crowded colloid systems with the atomic scale motions and forces that dictate elements of protein flexibility and selectivity. Because the PI are seeking to find agreement between two extremes of observable phenomena, a multidisciplinary approach is required; including but not limited to studying the bulk macromolecular phenomena that are indicative of the state of protein structure dynamics, such as reaction kinetics, static structure spectroscopy and colloid physics. The PI will then correlate these findings with investigations with novel techniques in 2d spectroscopy and molecular dynamics modeling to investigate pico-scale spatial and temporal phenomena, stopping short of regions where quantum effects begin to complicate observations.This project has implications for biofuel and for several fields outside of alternative energy, such as: home-personal care, waste management and medicine, possibly reducing the chemicals consumed for various applications by taking advantage of synergies between them and protein structural conformation dynamics. The PI will use this project to train and engage undergraduate students, particularly those from targeted groups, who have become attracted to such Green projects. In as much as this has yet to be substantiated, this broad interdisciplinary scope of investigation, coupled with emerging instrumental techniques, and prospective implications to the tangent fields mentioned above, mark this project as a ?high risk and high reward? situation, and an appropriate EAGER submission.