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Article Dans Une Revue Journal of Physical Chemistry B Année : 2011

H/D Isotope Effects in Protein Thermal Denaturation: The Case of Bovine Serum Albumin

Ling Fu
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Sandrine Villette
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Stéphane Petoud

Résumé

The present work investigates the effects of HID isotopic sub stitution on the structural and thermodynamic stability of bovine serum albumin (BSA) in aqueous solution over the temperature range of 5-90 degrees C. Using far-ultraviolet circular dichroism, we have compared protein unfolding pathways in H(2)O and D(2)O. Our results show that BSA possesses similar conformations in H(2)O and D(2)O at temperatures below 50 degrees C but follows different unfolding pathways at higher temperatures. The presence of D(2)O retards the occurrence of irreversible thermal denaturation in BSA, as evidenced by a higher onset temperature of 58 degrees C, in contrast to 50 degrees C in H(2)O center dot D(2)O exhibits a protective effect on the domain structure during the early stages of domain denaturation. Following incubation at 90 degrees C over a period of minutes, D(2)O causes a rapid aggregation of BSA molecules. This behavior is not observed in H(2)O solutions. Meanwhile, H/D substitution does not influence the reversible structural transformation of the protein in a significant manner. Partly renatured BSA in H(2)O and D(2)O undergoes very similar reversible structural transformations during a second heating cycle.
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Dates et versions

hal-00614896 , version 1 (17-08-2011)

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Citer

Ling Fu, Sandrine Villette, Stéphane Petoud, Felix Fernandez-Alonso, Marie-Louise Saboungi. H/D Isotope Effects in Protein Thermal Denaturation: The Case of Bovine Serum Albumin. Journal of Physical Chemistry B, 2011, 115 (8), pp.1881-1888. ⟨10.1021/jp104769v⟩. ⟨hal-00614896⟩
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