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- W1887435930 abstract "Publisher Summary Acidic fibroblast growth factor (aFGF) is the only member that is able to bind with high affinity to all four characterized FGF receptors (FGFRs), and variants produced by alternative mRNA splicing. In addition to an apparently low thermal stability, FGF appears to face additional problems in maintaining its native, functional structure. Human aFGF contains three cysteine residues and the related basic FGF (bFGF) contains four cysteines. This chapter focuses on the thermodynamic and structural studies of human aFGF and its relationship to the utilization of stability as a regulatory control mechanism for this growth factor. Structural analysis of human aFGF shows that the three free cysteine residues are located at solvent inaccessible positions. Thus, formation of mixed disulfides would be expected to destabilize the protein because structural changes would be required to expose the cysteines for oxidation, and covalent adducts of the cysteine residues would have to be tolerated within the packing constraints of the interior of the protein for the native state to be adopted. Human aFGF related basic FGF (bFGF) contains four cysteines. These residues are present in the active protein as free cysteine residues and oxidation, to form either inter- or intra-chain disulfide bonds, has been demonstrated to inactivate the protein." @default.
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- W1887435930 date "1997-01-01" @default.
- W1887435930 modified "2023-10-13" @default.
- W1887435930 title "Biophysical and structural analysis of human acidic fibroblast growth factor" @default.
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- W1887435930 doi "https://doi.org/10.1016/s1080-8914(97)80073-7" @default.
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