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dc.date.accessioned2013-03-12T08:36:08Z
dc.date.available2013-03-12T08:36:08Z
dc.date.issued2005en_US
dc.date.submitted2005-09-08en_US
dc.identifier.citationHaugen, Helen Sophie. The Three-Dimensional NMR-Structure of the Membrane-Permeabilizing Pediocin-Like Antimicrobial Peptide Curvacin A in Lipid Micelles. Hovedoppgave, University of Oslo, 2005en_US
dc.identifier.urihttp://hdl.handle.net/10852/11365
dc.description.abstractAntimicrobial peptides produced by lactic acid bacteria (LAB) are extensively studied, but little is know about their three-dimensional structures. Solution structures of these peptides will be useful to gain information about their mode of action, which again is important for further use of these substances in industry and medicine. Curvacin A is an antimicrobial peptide that belongs to the family of pediocin-like bacteriocins. Curvacin A was produced from its natural LAB producer, Lactobacillus curvatus LTH1174, and purified by ion-exchange- and reverse phase chromatography. Circular Dichroism-experiments revealed that curvacin A was unstructured in water, but became structured upon interactions with membrane-mimicking environments such as dodecyl phosphocholin (DPC)-micelles. The three-dimensional structure of curvacin A in DPC-micelles has been elucidated by the use of nuclear magnetic resonance (NMR)-spectroscopy. Curvacin A was shown to contain three regions: an N-terminal S-shaped ƒÒ-sheet like domain (residues 2-15), a central polar helix (residues 19-24) and an amphiphilic C-terminal helix (residues 29-39). The C-terminal tail consists of only two residues (G40 and M41) and seems to be unstructured. There was a hinge between the three regions, enabling the regions to move relative to each other.nor
dc.language.isoengen_US
dc.subjectmolekylærbiologi curvacin bakteriosin antimikrobial peptid NMR strukturbestemmelse melkesyre bakterieren_US
dc.titleThe Three-Dimensional NMR-Structure of the Membrane-Permeabilizing Pediocin-Like Antimicrobial Peptide Curvacin A in Lipid Micellesen_US
dc.typeMaster thesisen_US
dc.date.updated2005-10-14en_US
dc.creator.authorHaugen, Helen Sophieen_US
dc.subject.nsiVDP::476en_US
dc.identifier.bibliographiccitationinfo:ofi/fmt:kev:mtx:ctx&ctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:dissertation&rft.au=Haugen, Helen Sophie&rft.title=The Three-Dimensional NMR-Structure of the Membrane-Permeabilizing Pediocin-Like Antimicrobial Peptide Curvacin A in Lipid Micelles&rft.inst=University of Oslo&rft.date=2005&rft.degree=Hovedoppgaveen_US
dc.identifier.urnURN:NBN:no-11206en_US
dc.type.documentHovedoppgaveen_US
dc.identifier.duo30145en_US
dc.contributor.supervisorPer Eugen Krisitansen, Jon Nisse-Meyeren_US
dc.identifier.bibsys051855267en_US
dc.identifier.fulltextFulltext https://www.duo.uio.no/bitstream/handle/10852/11365/1/Oppgave20_07_05.pdf


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