T-4 Lysozyme as a Model for Protein Folding

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The goal of this project is to understand in greater detail the interrelationships of protein structure, stability and dynamics. T4 lysozyme is the protein used as a model. This moderate sized protein has a known 3-dimensional structure. Many mutant proteins of this lysozyme exist whose thermodynamic stability is modulated by the composition. Dr. Dahlquist has developed a plasmid expression system which allows large amounts of isotopically substituted protein to be produced efficiently. He will use modern nuclear magnetic resonance to study such proteins. The question of how proteins fold is acknowledged as one of the most important and least understood of modern molecular biology. A number of related areas would be greatly enhanced by the ability to understand in detail why a particular amino acid sequence folds into a particular shape and how changes in sequence change that shape, its thermodynamic stability and its interaction potential with other ligands. Progress in the understanding of the folding problem may allow more reliable predictions of structure from sequence data with a corresponding increase in the sophistication of engineered protein products.