Show simple item record Li, Xing en_US 2007-06-01T19:20:16Z 2007-06-01T19:20:16Z 1999-11-01T00:00:00Z en_US
dc.description.abstract Alamethicin is an _-aminoisobutyric acid-containing antibiotic produced by the soil fungus 'Trichoderma viride'. It forms voltage-dependent ion channels in lipid with multiple conductance levels. Unlabeled and 15N labeled alamethicin dimers were synthesized in which two monomers are linked at their C-terminal ends by a flexible linker. Electrospray ionization mass spectrometry confirmed the identity of the dimers purified by high-performance liquid chromatography. The structure and dynamics of alamethicin dimers were studied by carrying out extensive nuclear magnetic resonance spectroscopy and circular dichroism experiments. The results suggest that the entire peptide exists in a helical conformation, the N-terminus (Aib1-Aib10) has a more stable helical structure than the C-terminus (Val15-Pho 20) and a flexible structure in the middle (Gly11-Pro 14) connects the helices. The results also suggest that the C-terminal helices associate but the N-termini do not and support a gating mechanism that undergoes a voltage-dependent conformational rearrangement of the peptide with respect to the bilayer. (Abstract shortened by UMI.) en_US
dc.format.extent 5900483 bytes
dc.format.extent 184 bytes
dc.format.mimetype application/pdf
dc.format.mimetype text/plain
dc.language en en_US
dc.language.iso en_US
dc.rights info:eu-repo/semantics/openAccess
dc.title Structure and dynamics of alamethicin dimers by high-resolution proton and nitrogen-15 NMR spectroscopy en_US
dc.type info:eu-repo/semantics/masterThesis
dc.type master thesis en_US Chemistry en_US Master of Science (M.Sc.) en_US

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