Calorimetric indication of the molten globule-like state of cytochrome c induced by n-alkyl sulfates at low concentrations

The molten globule state has been proposed as a major intermediate of protein folding. However it has proven difficult to obtain thermodynamic data characterizing this state. To explore an alternative approach for characterization of the molten globule state, n-alkyl sulfates induced formation of th...

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Bibliographic Details
Published in:The Journal of chemical thermodynamics Vol. 35; no. 2; pp. 199 - 207
Main Authors: Chamani, J, Moosavi-Movahedi, A.A, Saboury, A.A, Gharanfoli, M, Hakimelahi, G.H
Format: Journal Article
Language:English
Published: Kidlington Elsevier Ltd 01-02-2003
Elsevier
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Summary:The molten globule state has been proposed as a major intermediate of protein folding. However it has proven difficult to obtain thermodynamic data characterizing this state. To explore an alternative approach for characterization of the molten globule state, n-alkyl sulfates induced formation of the molten globule state of horse cytochrome c at pH 2 was studied by isothermal titration calorimetry (ITC). Titration of the acid unfolded state of cytochrome c with sodium octyl sulfate, sodium dodecyl sulfate or sodium tetradecyl sulfate, generated an exothermic reaction for formation of the molten globule state. The effects of various n-alkyl sulfates on the acid unfolded state of cytochrome c demonstrated that the increased alkyl chain length enhanced the exothermic values of calorimetric enthalpy and induced a more compact molten globule states. The heat contents agreed well with the conformational transition measured by molar ellipticity at 222 nm ([ θ] 222) and Stoke radius ( Rs) values. These results emphasize that isothermal titration calorimetry provides a reasonable alternative method for characterization of the molten globule state.
ISSN:0021-9614
1096-3626
DOI:10.1016/S0021-9614(02)00312-9