| Structural Characterization of Hydroperoxide Lyase in Dodecyl Maltoside by Using Circular Dichroism. | |
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MedLine Citation:
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PMID: 23076732 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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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. |
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Authors:
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I Panagakou; E Touloupakis; D F Ghanotakis |
Publication Detail:
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Type: JOURNAL ARTICLE Date: 2012-10-18 |
Journal Detail:
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Title: The protein journal Volume: - ISSN: 1875-8355 ISO Abbreviation: Protein J. Publication Date: 2012 Oct |
Date Detail:
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Created Date: 2012-10-18 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 101212092 Medline TA: Protein J Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
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Department of Chemistry, University of Crete, P.O. Box 2208, 71003, Voutes-Heraklion, Greece. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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