Structural characterization of hydroperoxide lyase in dodecyl maltoside by using circular dichroism.

I Panagakou, E Touloupakis, D F Ghanotakis

The protein journal 2013 Jan

filter terms:

Fatty acid hydroperoxide lyase (HPL) is a membrane protein, member of the lipoxygenase pathway, which holds a central role in plant defense. Green bell pepper fatty acid hydroperoxide lyase, overexpressed in Escherichia coli, was purified and solubilized in two different non ionic detergents, Triton X-100 and dodecyl maltoside (DM). DM is considered to be more useful compared to Triton X-100, as it allows characterization of the protein with spectroscopic techniques, for which Triton X-100 was inapplicable. Circular dichroism demonstrated that HPL's secondary structure in DM consists of 13.53 % α-helix, 32.73 % β-sheet, 21.76 % turn and 31.13 % unordered.

Citation

I Panagakou, E Touloupakis, D F Ghanotakis. Structural characterization of hydroperoxide lyase in dodecyl maltoside by using circular dichroism. The protein journal. 2013 Jan;32(1):1-6