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- Title
Structural Characterization of Hydroperoxide Lyase in Dodecyl Maltoside by Using Circular Dichroism.
- Authors
Panagakou, I.; Touloupakis, E.; Ghanotakis, D.
- Abstract
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.
- Subjects
HYDROPEROXIDE lyase; CIRCULAR dichroism; MOLECULAR structure; FATTY acids; MEMBRANE proteins; LIPOXYGENASES; PLANT defenses
- Publication
Protein Journal, 2013, Vol 32, Issue 1, p1
- ISSN
1572-3887
- Publication type
Article
- DOI
10.1007/s10930-012-9454-1