Structure of lysozyme dissolved in neat organic solvents as assessed by NMR and CD spectroscopies
- Massachusetts Inst. of Tech., Cambridge, MA (United States). Dept. of Chemistry
- Rowland Inst. for Science, Cambridge, MA (United States)
The structure of the model protein hen egg-white lysozyme dissolved in water and in five neat organic solvents (ethylene glycol, methanol, dimethylsufloxide (DMSO), formamide, and dimethylformamide (DMF)) has been examined by means of {sup 1}H NMR and circular dichroism (CD) spectroscopies. The NMR spectra of lysozyme reveal the lack of a defined tertiary structure in all five organic solvents, although the examination of line widths suggests the possibility of some ordered structure in ethylene glycol and in methanol. The near-UV CD spectra of the protein suggest no tertiary structure in lysozyme dissolved in DMSO, formamide, and DMF, while a distinctive tertiary structure is seen in ethylene glycol and a drastically changed one in methanol. A highly developed secondary structure was observed by far-UV CD in ethylene glycol and methanol; interestingly, the {alpha}-helix content of the protein in both was greater than in water, while the {beta}-structure content was lower.
- Sponsoring Organization:
- USDOE, Washington, DC (United States); Massachusetts Inst. of Tech., Cambridge, MA (United States)
- OSTI ID:
- 347677
- Journal Information:
- Biotechnology and Bioengineering, Vol. 63, Issue 2; Other Information: PBD: 20 Apr 1999
- Country of Publication:
- United States
- Language:
- English
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