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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Published in: | The Journal of chemical thermodynamics Vol. 35; no. 2; pp. 199 - 207 |
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Main Authors: | , , , , |
Format: | Journal Article |
Language: | English |
Published: |
Kidlington
Elsevier Ltd
01-02-2003
Elsevier |
Subjects: | |
Online Access: | Get full text |
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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. |
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ISSN: | 0021-9614 1096-3626 |
DOI: | 10.1016/S0021-9614(02)00312-9 |