Chemical Denaturation Of The Elongation Factor 1 Alpha Isolated From The Hyperthermophilic Archaeon Sulfolobus Solfataricus(543 views) Granata V, Graziano G, Ruggiero A, Raimo G, Masullo M, Arcari P, Vitagliano L, Zagari A
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2006 Jan 24; 45(3): 719-726.
Keywords: Biochemistry, Cells, Fluorescence, Microorganisms, Urea, Denaturation, Electrostatic Interactions, Guanidine Hydrochloride (guhcl), Living Conditions, Proteins, Elongation Factor 1alpha, Guanosine Diphosphate, Nucleotide, Article, Circular Dichroism, Electricity, Nonhuman, Priority Journal, Protein Analysis, Protein Denaturation, Protein Stability, Protein Structure, Sulfolobus Solfataricus, Bacterial Proteins, Enzyme Stability, Peptide Elongation Factor 1, Protein Conformation, Thermodynamics, Archaea,
Affiliations: *** IBB - CNR ***
Dipartimento delle Scienze Biologiche, Sezione di Biostrutture, Università degli Studi di Napoli Federico II, I-80134 Napoli, Italy
Dipartimento di Scienze Biologiche ed Ambientali, Università del Sannio, I-82100 Benevento, Italy
Dipartimento di Biochimica e Biotecnologie Mediche, Università degli Studi di Napoli Federico II, I-80131 Napoli, Italy
Istituto di Biostrutture e Bioimmagini, CNR, I-80134 Napoli, Italy
Centro Interuniversitario di Ricerca sui Peptidi Bioattivi (CIRPEB), I-80134 Napoli, Italy
References: Not available.
Chemical Denaturation Of The Elongation Factor 1 Alpha Isolated From The Hyperthermophilic Archaeon Sulfolobus Solfataricus
The stability against chemical denaturants of the elongation factor EF-1 alpha (SsEF-1 alpha), a protein isolated from the hyperthermophilic archaeon Sulfolobus solfataricus has been characterized in detail. Indeed, the atypical shape of the protein structure and the unusual living conditions of the host organism prompted us to analyze the effect of urea and guanidine hydrochloride (GuHCl) on the GDP complex of the enzyme (SsEF-1 alpha (.) GDP) by fluorescence and circular dichroism. These studies were also extended to the nucleotide-free form of the protein (nfSsEF-1 alpha). Interestingly, the experiments show that the denaturation, curves of both SsEF-1 alpha forms present a single inflection point, which is indicative of a cooperative unfolding process with no intermediate species. Moreover, the chemically induced unfolding process of both SsEF1 alpha (.) GDP and nfSsEF-1 alpha is fully reversible. Both SsEF-1 alpha forms exhibit remarkable stability against urea, but they do not display a strong resistance to the denaturing action of GuHCl. These findings suggest that electrostatic interactions significantly contribute to SsEF-1 alpha stability
Chemical Denaturation Of The Elongation Factor 1 Alpha Isolated From The Hyperthermophilic Archaeon Sulfolobus Solfataricus