Details
| Original language | English |
|---|---|
| Pages (from-to) | 343-349 |
| Number of pages | 7 |
| Journal | Biochemical Journal |
| Volume | 335 |
| Issue number | 2 |
| Publication status | Published - 15 Oct 1998 |
| Externally published | Yes |
Abstract
The conformational stability and the folding properties of the all-β-type protein human basic fibroblast growth factor (hFGF-2) were studied by means of fluorescence spectroscopy. The results show that the instability of the biological activity of hFGF-2 is also reflected in a low conformational stability of the molecule. The reversibility of the unfolding and refolding process was established under reducing conditions. Determination of the free-energy of unfolding in the presence of reducing agents revealed that the conformational stability of hFGF-2 (ΔG(app)(H2O) ≃ 21 kJ·mol-1, 25°C) is low compared with other globular proteins under physiological conditions (20-60 kJ·mol-1). However, the conformational stability of hFGF-2 is particularly low under non-reducing conditions. This instability is attributed to intramolecular disulphide-bond formation, rendering the molecule more susceptible to denaturant-induced unfolding. In addition, denaturant-induced unfolding of hFGF-2 renders the protein more susceptible to irreversible oxidative denaturation. Experimental evidence is provided that the irreversibility of the unfolding and refolding process in the absence of reducing agents is linked to the formation of an intramolecular disulphide bond involving cysteines 96 and 101.
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Biology
- Biochemistry, Genetics and Molecular Biology(all)
- Cell Biology
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In: Biochemical Journal, Vol. 335, No. 2, 15.10.1998, p. 343-349.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Susceptibility towards intramolecular disulphide-bond formation affects conformational stability and folding of human basic fibroblast growth factor
AU - Estapé, David
AU - Van Den Heuvel, Joop
AU - Rinas, Ursula
PY - 1998/10/15
Y1 - 1998/10/15
N2 - The conformational stability and the folding properties of the all-β-type protein human basic fibroblast growth factor (hFGF-2) were studied by means of fluorescence spectroscopy. The results show that the instability of the biological activity of hFGF-2 is also reflected in a low conformational stability of the molecule. The reversibility of the unfolding and refolding process was established under reducing conditions. Determination of the free-energy of unfolding in the presence of reducing agents revealed that the conformational stability of hFGF-2 (ΔG(app)(H2O) ≃ 21 kJ·mol-1, 25°C) is low compared with other globular proteins under physiological conditions (20-60 kJ·mol-1). However, the conformational stability of hFGF-2 is particularly low under non-reducing conditions. This instability is attributed to intramolecular disulphide-bond formation, rendering the molecule more susceptible to denaturant-induced unfolding. In addition, denaturant-induced unfolding of hFGF-2 renders the protein more susceptible to irreversible oxidative denaturation. Experimental evidence is provided that the irreversibility of the unfolding and refolding process in the absence of reducing agents is linked to the formation of an intramolecular disulphide bond involving cysteines 96 and 101.
AB - The conformational stability and the folding properties of the all-β-type protein human basic fibroblast growth factor (hFGF-2) were studied by means of fluorescence spectroscopy. The results show that the instability of the biological activity of hFGF-2 is also reflected in a low conformational stability of the molecule. The reversibility of the unfolding and refolding process was established under reducing conditions. Determination of the free-energy of unfolding in the presence of reducing agents revealed that the conformational stability of hFGF-2 (ΔG(app)(H2O) ≃ 21 kJ·mol-1, 25°C) is low compared with other globular proteins under physiological conditions (20-60 kJ·mol-1). However, the conformational stability of hFGF-2 is particularly low under non-reducing conditions. This instability is attributed to intramolecular disulphide-bond formation, rendering the molecule more susceptible to denaturant-induced unfolding. In addition, denaturant-induced unfolding of hFGF-2 renders the protein more susceptible to irreversible oxidative denaturation. Experimental evidence is provided that the irreversibility of the unfolding and refolding process in the absence of reducing agents is linked to the formation of an intramolecular disulphide bond involving cysteines 96 and 101.
UR - http://www.scopus.com/inward/record.url?scp=0032532007&partnerID=8YFLogxK
U2 - 10.1042/bj3350343
DO - 10.1042/bj3350343
M3 - Article
C2 - 9761733
AN - SCOPUS:0032532007
VL - 335
SP - 343
EP - 349
JO - Biochemical Journal
JF - Biochemical Journal
SN - 0264-6021
IS - 2
ER -