Abstract
Protein sequences encode the information required to form specific three-dimensional structures (Anfinsen, 1973), but it is still not possible to predict protein structure and function from sequence information alone. It is possible, however, to understand the relationship among the structure, function, and sequence of some proteins. Our laboratory has been using genetic and biochemical approaches to define the determinants of protein structure and function for two sequence-specific DNA-binding proteins, the cI repressor and Cro protein of bacteriophage X. We have been able to identify residues that play key roles in maintaining the folded structures of these proteins and residues that allow these proteins to bind specifically to operator DNA. Our interest has also been focused on the factors that determine intracellular protein turnover, since many mutant Cro proteins, but not mutant cl repressors, are hypersensitive to degradation. In this chapter, we review these studies and describe how intragenic, second-site reversion has been used to identify amino acid substitutions that enhance protein function.
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References
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© 1987 Plenum Press, New York
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Sauer, R.T., Nelson, H.C.M., Hecht, M.H., Pakula, A. (1987). Identifying the Determinants of Protein Function and Stability. In: Poste, G., Crooke, S.T. (eds) New Frontiers in the Study of Gene Functions. New Horizons in Therapeutics. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-1845-3_14
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DOI: https://doi.org/10.1007/978-1-4613-1845-3_14
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