SOLID STATE STRUCTURAL NMR OF LH1 PROTEIN

The last decade has witnessed a remarkable growth of knowledge in structural biology. A class of protein particularly important for biological energy transduction, membrane proteins, has begun to yield structural information by high-resolution methods. These developments notwithstanding, our current knowledge-base of membrane-protein structure is very limited; 103 globular protein structures have been reported, but only 101 membrane protein structures are known. Furthermore, consider that approximately 30 percent of structural genes in a free-living microbe are believed to encode membrane proteins, and one concludes that membrane protein structure is an important area of structural biology that has been overlooked. Likewise, detailed examination of the molecular forces that fold and stabilize membrane proteins has lagged behind globular proteins. The Applicant proposes to undertake novel approaches to these problems with solid state NMR spectroscopy. The high resolution structure and dynamics of an oligomeric membrane protein, the LH1 light-harvesting complex from photosynthetic bacteria, will be studied.