Stability Against Temperature Of Sulfolobus Solfataricus Elongation Factor 1 Alpha, A Multi-Domain Protein(642 views) Granata V, Graziano G, Ruggiero A, Raimo G, Masullo M, Arcari P, Vitagliano L, Zagari A
Keywords: Archaea, Circular Dichroism, Elongation Factor, Fluorescence, Protein Stability, Thermal Denaturation, Bacterial Protein, Elongation Factor 1alpha, Article, Controlled Study, Escherichia Coli, Nonhuman, Ph Measurement, Priority Journal, Protein Analysis, Protein Denaturation, Protein Isolation, Sulfolobus Solfataricus, Temperature Sensitivity, Thermostability, Archaeal Proteins, Guanosine Diphosphate, Hydrogen-Ion Concentration, Peptide Elongation Factor 1, Protein Binding, Protein Folding, Protein Structure, Secondary, Tertiary,
Affiliations: *** IBB - CNR ***
Dip. delle Scienze Biologiche, Sez. di Biostrutture, Università degli Studi di Napoli Federico II, Napoli, Italy
CNISM, Università degli Studi di Napoli Federico II, Napoli, Italy
Dip. di Scienze Biologiche ed Ambientali, Università del Sannio, Benevento, Italy
Istituto di Biostrutture e Bioimmagini, CNR, Napoli, Italy
CIRPEB, Napoli, Italy
Dip. di Scienze e Tecnologie per l'Ambiente e il Territorio, Università degli Studi del Molise, Isernia, Italy
Dip. di Biochimica e Biotecnologie Mediche, Università degli Studi di Napoli Federico II, Napoli, Italy
Dip. di Scienze Farmacobiologiche, Università degli Studi Magna Graecia di Catanzaro, Roccelletta di Borgia, Catanzaro, Italy
CEINGE-Biotecnologie Avanzate, Scarl, Napoli, Italy
CNISM, Universit degli Studi di Napoli Federico II, Napoli, Italy
References: Not available.
Stability Against Temperature Of Sulfolobus Solfataricus Elongation Factor 1 Alpha, A Multi-Domain Protein
The elongation factors (EF-Tu/EF-1 alpha) are universal proteins, involved in protein biosynthesis. A detailed characterization of the stability against temperature of SsEF-1 alpha, a three-domain protein isolated from the hyperthermophilic archaeon Sulfolobus solfataricus is presented. Thermal denaturation of both the GDP-bound (SsEF-1 alpha center dot GDP) and the ligand-free (nfSsEF-1 alpha) 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-1 alpha play a role also at high temperatures. Finally, it is shown that the enzyme exhibits two different interchangeable thermally denatured states, depending on pH. (0 2008 Elsevier B. V All rights reserved
Stability Against Temperature Of Sulfolobus Solfataricus Elongation Factor 1 Alpha, A Multi-Domain Protein
Aloj L, Aurilio M, Rinaldi V, D'Ambrosio L, Tesauro D, Peitl PK, Maina T, Mansi R, Von Guggenberg E, Joosten L, Sosabowski JK, Breeman WA, De Blois E, Koelewijn S, Melis M, Waser B, Beetschen K, Reubi JC, De Jong M * The EEE project(561 views) Proc Int Cosm Ray Conf Icrc Universidad Nacional Autonoma De Mexico, 2007; 5(HEPART2): 977-980. Impact Factor:0 ViewExport to BibTeXExport to EndNote