Journal
BIOMACROMOLECULES
Volume 11, Issue 11, Pages 2944-2948Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bm100735z
Keywords
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Funding
- NSF
- Department of Energy Office of Basic Energy Science
- Direct For Mathematical & Physical Scien
- Division Of Materials Research [820506] Funding Source: National Science Foundation
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The dissolution and dissolved molecular state of cytochrome c were investigated in the room temperature ionic liquid ethylmethylimidazolium ethylsulfate, [EMIM][E1SO(4)]. by viscometry, optical and vibrational spectroscopies, and peroxidase activity. In dilute mixtures, viscometry demonstrated true molecular dissolution of cytochrome c in the ionic liquid and uncovered a molecular size larger than that in aqueous buffer, suggesting altered solvation or slight denaturation. The protein's heme unit absorbs light outside the spectral range masked by [EMIM] enabling conformational assessments by UV-visible and circular dichroism spectroscopies. Adding trends from fluorescence and Fourier transform infrared spectroscopy, unchanged secondary but perturbed tertiary structures were determined, consistent with the appreciable peroxidase activity measured. Different than in aqueous buffers, denaturation is not accompanied by aggregation. Results are relevant to the proposed application of ionic liquids as media for room temperature preservation of biomacromolecules.
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