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dc.contributor.author Whiles-Lillig, Jennifer en
dc.contributor.author Glover, Kerney J. en
dc.contributor.author Vold, Regitze R. en
dc.contributor.author Komives, Elizabeth A. en
dc.date.accessioned 2012-07-31T16:23:09Z en
dc.date.available 2012-07-31T16:23:09Z en
dc.date.issued 2002 en
dc.identifier.citation J. Whiles, K. Glover, R.R. Vold, and E. Komives. "Methods for studying transmembrane peptides in bicelles: Consequences of hydrophobic mismatch and peptide sequence." J. Mag. Res. 158, 149-156 (2002). en
dc.identifier.uri http://hdl.handle.net/10211.1/1509 en
dc.description Published by and copyright of Elsevier. en
dc.description.abstract We have shown that bicelles prepared from dilauryl phosphatidylcholine (DLPC) and dipalmitoyl phosphatidylcholine (DPPC) align in a magnetic field under conditions similar to the more common dimyristoyl phosphatidylcholine (DMPC) bicelles. In addition, a model transmembrane peptide, P16, with a hydrophobic stretch of 24 AA, and specific alanine-d3 labels, was incorporated into all of the different bicelles. The long-chain phospholipid (DLPC, DMPC, or DPPC) remained unperturbed upon incorporation of the peptide while the quadrupolar splitting of the short-chain phospholipid along the bicelle rim increased by varying degrees in the different bicelle systems. The change in quadrupolar splitting of the short-chain phospholipids was attributed to changes in either fluidity of the planar region of the bicelle or differences in overall lipid packing. When the hydrophobic stretch of the bilayer was 22.8 (DMPC) or 26.3 A (DPPC), the peptide tilt was found to be transmembrane (33–35 degrees with respect to the bicelle normal). When the hydrophobic stretch of the bilayer was 19.5 A (DLPC), the peptide quadrupolar splittings suggested a loss of transmembrane orientation. When tryptophan was incorporated in the middle of the transmembrane region, the transmembrane orientation was also lost. en
dc.description.sponsorship Whiles-Lillig was funded by a La Jolla Interfaces in Science predoctoral fellowship through the Burroughs Wellcome Fund. en
dc.description.uri Publisher's definitive version is available from Elsevier Science at http://www.journals.elsevier.com/journal-of-magnetic-resonance/ en
dc.language.iso en_US en
dc.publisher Journal of Magnetic Resonance en
dc.subject bicelles en
dc.subject transmembrane peptide en
dc.title Methods for Studying Transmembrane Peptides in Bicelles: Consequences of Hydrophobic Mismatch and Peptide Sequence en
dc.type Book en
dc.relation.journal Journal of Magnetic Resonance en
dc.contributor.sonomaauthor Whiles-Lillig, Jennifer en

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