At high concentration (98% or higher, v/v), glycerol induces collapse of acid-denatured cytochrome c into a compact state, the G(U) state, showing a molten globule character. The G(U) state possesses a nativelike a-helix structure but a tertiary conformation less packed with respect to the native state. The spectroscopic properties of the G(U) state closely resemble those of the molten globule stabilized by the organic solvent from the native protein (called the G(N) state), indicating that glycerol can stabilize the molten globule of cytochrome c either from the native or the acid-denatured protein. The G(U) and the G(N) states show spectroscopic (and, thus, structural) properties and stabilities comparable to those of molten globules stabilized by different effectors, despite the fact that the mechanisms involved in the molten globule formation may significantly differ. This implies in cytochrome c a hierarchy for the rupture (native-to-molten globule) or the formation (unfolded-to-molten globule) of intramolecular interactions leading to the stabilization of the molten globule state of the protein, independently from the effector responsible for the structural transition, in accord with the sequential model proposed by Englander and collaborators.

Bongiovanni, C., Sinibaldi, F., Ferri, T., Santucci, R. (2002). Glycerol-induced formation of the molten globule from acid-denatured cytochrome c: Implication for hierarchical folding. JOURNAL OF PROTEIN CHEMISTRY, 21(1), 35-41 [10.1023/A:1014179031881].

Glycerol-induced formation of the molten globule from acid-denatured cytochrome c: Implication for hierarchical folding

SINIBALDI, FEDERICA;SANTUCCI, ROBERTO
2002-01-01

Abstract

At high concentration (98% or higher, v/v), glycerol induces collapse of acid-denatured cytochrome c into a compact state, the G(U) state, showing a molten globule character. The G(U) state possesses a nativelike a-helix structure but a tertiary conformation less packed with respect to the native state. The spectroscopic properties of the G(U) state closely resemble those of the molten globule stabilized by the organic solvent from the native protein (called the G(N) state), indicating that glycerol can stabilize the molten globule of cytochrome c either from the native or the acid-denatured protein. The G(U) and the G(N) states show spectroscopic (and, thus, structural) properties and stabilities comparable to those of molten globules stabilized by different effectors, despite the fact that the mechanisms involved in the molten globule formation may significantly differ. This implies in cytochrome c a hierarchy for the rupture (native-to-molten globule) or the formation (unfolded-to-molten globule) of intramolecular interactions leading to the stabilization of the molten globule state of the protein, independently from the effector responsible for the structural transition, in accord with the sequential model proposed by Englander and collaborators.
2002
Pubblicato
Rilevanza internazionale
Articolo
Sì, ma tipo non specificato
Settore BIO/10 - BIOCHIMICA
English
Con Impact Factor ISI
Circular dichroism; Cytochrome c; Glycerol; Molten globule
Bongiovanni, C., Sinibaldi, F., Ferri, T., Santucci, R. (2002). Glycerol-induced formation of the molten globule from acid-denatured cytochrome c: Implication for hierarchical folding. JOURNAL OF PROTEIN CHEMISTRY, 21(1), 35-41 [10.1023/A:1014179031881].
Bongiovanni, C; Sinibaldi, F; Ferri, T; Santucci, R
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/49765
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