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Ligand‐free form of human α‐fetoprotein: evidence for the molten globule state
Author(s) -
Uversky Vladimir N,
Narizhneva Natalya V,
Ivanova Tatyana V,
Kirkitadze Marina D,
Tomashevski Andrey Yu
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00606-6
Subject(s) - molten globule , ligand (biochemistry) , chemistry , free form , biophysics , biochemistry , biology , protein structure , computer science , receptor , computer graphics (images)
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.