Ligand-free Form of Human α-fetoprotein: Evidence for the Molten Globule State
Document Type
Article
Publication Date
1997
Digital Object Identifier (DOI)
https://doi.org/10.1016/S0014-5793(97)00606-6
Abstract
By means of circular dichroism and fluorescence spectroscopy, viscometry and scanning microcalorimetry we have shown that the release of ligands from human α-fetoprotein (AFP) results in a considerable rearrangement of the protein molecule. Ligand-free form is practically as compact as the native molecule and has native-like content of secondary structure but no rigid tertiary structure. This means that the release of ligands transforms the AFP molecule into a molten globule state. Stripping the ligands from AFP is the irreversible process, i.e., native protein molecule cannot be reconstituted from the ligand-free form of AFP by adding back ligands. A possible functional role of such a structural transformation is discussed.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
FEBS Letters, v. 410, issue 2-3, p. 280-284
Scholar Commons Citation
Uversky, Vladimir N.; Narizhneva, Natalya V.; Ivanova, Tatyana V.; Kirkitadze, Marina D.; and Tomashevsky, Andrey Yu., "Ligand-free Form of Human α-fetoprotein: Evidence for the Molten Globule State" (1997). Molecular Medicine Faculty Publications. 642.
https://digitalcommons.usf.edu/mme_facpub/642
