427687 The Structure and Function of Photosynthetic Protein Complexes: An Experimental and Computational Study

Wednesday, November 11, 2015
Exhibit Hall 1 (Salt Palace Convention Center)
Bradley Harris, Civil and Chemical Engineering, University of Tennessee, Chattanooga, Chattanooga, TN, Xiaolin Cheng, Oak Ridge National Laboratory, Oak Ridge, TN and Paul Frymier, Department of Chemical & Biomolecular Engineering, University of Tennessee, Knoxville, TN

Proteins mediate many biological functions and can possess a diverse set of features, all of which affect their interactions with other proteins, inorganic molecules, and surfaces. Gaining insight into proteins and their interactions is crucial to our understanding of the biological world, and could provide technological advancement in alternative energy, drug discovery, and a wealth of other areas. Membrane proteins are of particular interest, as they are responsible for mediating cell-environment interactions such as cellular recognition, signal transduction, and the transportation of ions and molecules across the membrane. Here, we are interested in studying photosystem I (PSI), a membrane integral protein involved in the photosynthetic cycle of plants and microorganisms that has been the subject of research for biorenewable energy conversion applications. We will present our work involving the use of a combination of small-angle neutron scattering and molecular dynamics simulation to study the structure and function of a PSI-detergent complex resulting from solubilization of this protein from its native membrane. We will also discuss current progress in studying the coupling of PSI with hydrogenase enzyme, which results in a unique complex capable of light-driven hydrogen production.

Extended Abstract: File Not Uploaded
See more of this Session: Poster Session: Bioengineering
See more of this Group/Topical: Food, Pharmaceutical & Bioengineering Division