Protein Structure and Folding at Low Temperature

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An understanding of how and why a protein folds into its native conformation is of major biological importance. Although much work has been done on this problem still relatively little is known about the details of the process. Dr. Fink is studying the factors which determine a particular folding pathway and hence native structure. The long-term goals are to learn the "rules" by which the amino acid sequence of a polypeptide guides the folding path to the native state. Dr. Fink will use: 1) specific signals or probes in different regions of the molecule to aid determining the order in which the protein folds and unfolds; 2) site-specific mutants to facilitate the formation of protein with environment-sensitive probes in unique and selected sites and probe the role of individual amino acids on the folding; and 3) subzero temperatures and aqueous-methanol cryosolvents to permit the stabilization and characterization of partially-folded intermediates in both unfolding and refolding.