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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2000-9-29
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pubmed:abstractText |
The amphipathic helix plays a key role in many membrane-associating peptides and proteins. The dynamics of helices on membrane surfaces might be of importance to their function. The fluorescence anisotropy decay of tryptophan is a sensitive indicator of local, segmental, and global dynamics within a peptide or protein. We describe the use of frequency domain dynamic depolarization measurements to determine the site-specific tryptophan dynamics of single tryptophan amphipathic peptides bound to a phospholipid surface. The five 18-residue peptides studied are based on a class A amphipathic peptide that is known to associate at the interface of phospholipid bilayers. The peptides contain a single tryptophan located at positions 2, 3, 7, 12, or 14 in the sequence. Association of the peptides with egg phosphatidylcholine vesicles results in complex behavior of both the tryptophan intensity decay and the anisotropy decay. The anisotropy decays were biphasic and were fitted to an associated model where each lifetime component in the intensity decay is associated with a particular rotational correlation time from the anisotropy decay. In contrast, an unassociated model where all components of the intensity decay share common rotational modes was unable to provide an adequate fit to the data. Two correlation times were resolved from the associated analysis: one whose contribution to the anisotropy decay was dependent on the exposure of the tryptophan to the aqueous phase, and the other whose contribution reflected the position of the tryptophan in the sequence. The results are compared with existing x-ray structural data and molecular dynamics simulations of membrane-incorporated peptides.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/10920036-10028238,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10920036-10354448,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10920036-10388560,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10920036-11525196,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10920036-2036384,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10920036-2176475,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10920036-2369871,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10920036-2690075,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10920036-3079525,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10920036-3132727,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10920036-3242631,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10920036-3580486,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10920036-3756174,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10920036-3781080,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10920036-3944133,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10920036-4504348,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10920036-6378065,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10920036-6885244,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10920036-7059650,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10920036-8394121,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10920036-8913686,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10920036-896960,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10920036-8994617,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10920036-9017204,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10920036-9237913,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10920036-9860871
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0006-3495
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
79
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1066-73
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:10920036-Amino Acid Sequence,
pubmed-meshheading:10920036-Fluorescence Polarization,
pubmed-meshheading:10920036-Lipid Bilayers,
pubmed-meshheading:10920036-Models, Molecular,
pubmed-meshheading:10920036-Molecular Sequence Data,
pubmed-meshheading:10920036-Peptides,
pubmed-meshheading:10920036-Phosphatidylcholines,
pubmed-meshheading:10920036-Protein Structure, Secondary,
pubmed-meshheading:10920036-Proteins,
pubmed-meshheading:10920036-Structure-Activity Relationship,
pubmed-meshheading:10920036-Tryptophan,
pubmed-meshheading:10920036-X-Ray Diffraction
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pubmed:year |
2000
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pubmed:articleTitle |
Site-specific tryptophan dynamics in class A amphipathic helical peptides at a phospholipid bilayer interface.
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pubmed:affiliation |
The Russell Grimwade School of Biochemistry and Molecular Biology, University of Melbourne, Parkville, 3052 Australia. clayton@mpc186.mpibpc.gwdg.de
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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