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Thermal unfolding of a double-domain protein / Ying Ren in Industrial & engineering chemistry research, Vol. 48 N° 19 (Octobre 2009) 

Public ISBD [article]  in Industrial & engineering chemistry research > Vol. 48 N° 19 (Octobre 2009) . - pp. 8865–8871 Titre : Thermal unfolding of a double-domain protein : molecular dynamics simulation of rhodanese Type de document : texte imprimé Auteurs : Ying Ren, Auteur ; Jian Gao, Auteur ; Wei Ge, Auteur Année de publication : 2009 Article en page(s) : pp. 8865–8871 Note générale : Chemical engineering Langues : Anglais (eng) Mots-clés : Bovine  liver  rhodanese  Explicit  solvent  molecular  dynamics  simulations Résumé : The thermal unfolding process of bovine liver rhodanese, composing two globular domains (N-domain and C-domain) with similar tertiary structures, has been studied by explicit solvent molecular dynamics (MD) simulations at high temperatures of 450 and 500 K, as well as 308 K for comparisons. The results are in good agreement with the available experimental results (Horowitz, P. M.; Butler, M. Interactive Intermediates Are Formed During the Urea Unfolding of Rhodanese. J. Biol. Chem. 1993, 268 (4), 2500−2504. Shibatani, T.; Kramer, G.; Hardesty, B.; Horowitz, P. M. Domain Separation Precedes Global Unfolding of Rhodanese. J. Biol. Chem. 1999, 274 (47), 33795−33799. Ybarra, J.; Bhattacharyya, A. M.; Panda, M.; Horowitz, P. M. Active Rhodanese Lacking Nonessential Sulfhydryl Groups Contains an Unstable C-Terminal Domain and Can Be Bound, Inactivated, and Reactivated by GroEL. J. Biol. Chem. 2003, 278 (3), 1693−1699). Besides that our simulation can also depict more dynamic details of the unfolding process. The solvent accessible surface area (SASA) shows a remarkable increase mainly due to a more exposed hydrophobic area, indicating that the hydrophobic interaction is considerably weaker at high temperatures. Comparisons between the thermal stabilities of equivalent secondary structures in both domains suggest that the C-domain is more fragile than the N-domain and the breaking down of the secondary structures follows the pattern [α-helix]→[bend, turn, 3-helix, and 5-helix]. Different regimes of unfolding intermediates have also been discussed. En ligne : http://pubs.acs.org/doi/abs/10.1021/ie801441x [article] Thermal unfolding of a double-domain protein : molecular dynamics simulation of rhodanese [texte imprimé] / Ying Ren, Auteur ; Jian Gao, Auteur ; Wei Ge, Auteur . - 2009 . - pp. 8865–8871. Chemical engineering Langues : Anglais (eng) in Industrial & engineering chemistry research > Vol. 48 N° 19 (Octobre 2009) . - pp. 8865–8871 Mots-clés : Bovine  liver  rhodanese  Explicit  solvent  molecular  dynamics  simulations Résumé : The thermal unfolding process of bovine liver rhodanese, composing two globular domains (N-domain and C-domain) with similar tertiary structures, has been studied by explicit solvent molecular dynamics (MD) simulations at high temperatures of 450 and 500 K, as well as 308 K for comparisons. The results are in good agreement with the available experimental results (Horowitz, P. M.; Butler, M. Interactive Intermediates Are Formed During the Urea Unfolding of Rhodanese. J. Biol. Chem. 1993, 268 (4), 2500−2504. Shibatani, T.; Kramer, G.; Hardesty, B.; Horowitz, P. M. Domain Separation Precedes Global Unfolding of Rhodanese. J. Biol. Chem. 1999, 274 (47), 33795−33799. Ybarra, J.; Bhattacharyya, A. M.; Panda, M.; Horowitz, P. M. Active Rhodanese Lacking Nonessential Sulfhydryl Groups Contains an Unstable C-Terminal Domain and Can Be Bound, Inactivated, and Reactivated by GroEL. J. Biol. Chem. 2003, 278 (3), 1693−1699). Besides that our simulation can also depict more dynamic details of the unfolding process. The solvent accessible surface area (SASA) shows a remarkable increase mainly due to a more exposed hydrophobic area, indicating that the hydrophobic interaction is considerably weaker at high temperatures. Comparisons between the thermal stabilities of equivalent secondary structures in both domains suggest that the C-domain is more fragile than the N-domain and the breaking down of the secondary structures follows the pattern [α-helix]→[bend, turn, 3-helix, and 5-helix]. Different regimes of unfolding intermediates have also been discussed. En ligne : http://pubs.acs.org/doi/abs/10.1021/ie801441x