| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1180578 | Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics | 2008 | 9 Pages |
Abstract
The elongation factors (EF-Tu/EF-1α) are universal proteins, involved in protein biosynthesis. A detailed characterization of the stability against temperature of SsEF-1α, a three-domain protein isolated from the hyperthermophilic archaeon Sulfolobus solfataricus is presented. Thermal denaturation of both the GDP-bound (SsEF-1α
- GDP) and the ligand-free (nfSsEF-1α) forms was investigated by means of circular dichroism and fluorescence measurements, over the 4.0-7.5 pH interval. Data indicate that the unfolding process is cooperative with no intermediate species and that the few inter-domain contacts identified in the crystal structure of SsEF-1α play a role also at high temperatures. Finally, it is shown that the enzyme exhibits two different interchangeable thermally denatured states, depending on pH.
- GDP) and the ligand-free (nfSsEF-1α) forms was investigated by means of circular dichroism and fluorescence measurements, over the 4.0-7.5 pH interval. Data indicate that the unfolding process is cooperative with no intermediate species and that the few inter-domain contacts identified in the crystal structure of SsEF-1α play a role also at high temperatures. Finally, it is shown that the enzyme exhibits two different interchangeable thermally denatured states, depending on pH.
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Vincenzo Granata, Giuseppe Graziano, Alessia Ruggiero, Gennaro Raimo, Mariorosario Masullo, Paolo Arcari, Luigi Vitagliano, Adriana Zagari,