Can we understand function in terms of protein structure and dynamics?
A number of protein systems have been studied to elucidate the link between chemistry, structure, dynamics and function. The system that has been studied the longest in my laboratory is E. coli thioredoxin, a long-standing collaboration with Professor Arne Holmgren of the Karolinska Institute, Sweden. This small (108-residue) thiol-disulfide oxidoreductase has a multitude of functions in the cell, including the vital process of ribonucleotide reduction to form deoxyribonucleotides for DNA synthesis. Thioredoxins occur in all living organisms and in viruses; mammalian thioredoxins have been shown to have a vital role in cellular control mechanisms and have recently been implicated in human disease processes: thioredoxin is found at elevated levels in the serum of AIDS patients. Thioredoxins are related structurally to protein disulfide isomerases, but differences in redox potential mean that there is a clear functional difference between the two. Indeed, one of the primary functions of
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