Circularly Permuted Dihydrofolate Reductase Possesses All the Properties of the Molten Globule State, But Can Resume Functional Tertiary Structure by Interaction with Its Ligands
Document Type
Article
Publication Date
1996
Digital Object Identifier (DOI)
https://doi.org/10.1002/pro.5560050910
Abstract
It is obvious that functional activity of a protein molecule is closely related to its structure. On the other hand, the understanding of structure-function relationship still remains one of the intriguing problems of molecular biology. There is widespread belief that mutagenesis presents a real way to solve this problem. Following this assumption, we have investigated the effect of circular permutation in dihydrofolate reductase from E. coli on protein structure and functioning. It has been shown that in the absence of ligands two circularly permuted variants of dihydrofolate reductase possess all the properties of the molten globule state. However, after addition of ligands they gain the native-like structural properties and specific activity. This means that the in vitro folding of permuted dihydrofolate reductase is terminated at the stage of the molten globule formation. Interaction of permuted protein with ligands leads to the structural adjustment and formation of active protein molecules.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
Protein Science, v. 5, issue 9, p. 1844-1851
Scholar Commons Citation
Uversky, Vladimir N.; Protasova, Natalya YU.; Rogov, Vladimir V.; Vassilenko, Konstantin S.; Gudkov, Anatoly T.; and Kutyshenko, Victor P., "Circularly Permuted Dihydrofolate Reductase Possesses All the Properties of the Molten Globule State, But Can Resume Functional Tertiary Structure by Interaction with Its Ligands" (1996). Molecular Medicine Faculty Publications. 639.
https://digitalcommons.usf.edu/mme_facpub/639
