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  Site-specific tryptophan fluorescence spectroscopy as a probe of membrane peptide structure and dynamics

Clayton, A. H. A., & Sawyer, W. H. (2002). Site-specific tryptophan fluorescence spectroscopy as a probe of membrane peptide structure and dynamics. European Biophysics Journal, 31(1), 9-13. Retrieved from http://springerlink.metapress.com/content/r6031fq97rue6y5b/fulltext.pdf.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-F424-5 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-E588-E
Genre: Journal Article

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17038.pdf (Publisher version), 0B
 
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Restricted (Max Planck Institute for Biophysical Chemistry (Karl Friedrich Bonhoeffer Institute), Göttingen; )
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 Creators:
Clayton, A. H. A.1, Author              
Sawyer, W. H., Author
Affiliations:
1Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society, ou_578628              

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Free keywords: tryptophan; dynamics; amphipathic helix; lipid-protein interactions; time-resolved fluorescence spectroscopy
 Abstract: The fluorescence from tryptophan contains valuable information about the environment local to the indole side-chain. This environment sensitivity coupled with the ability to synthetically or genetically incorporate a single tryptophan residue at specific sites in a polypeptide sequence has provided the membrane biophysicist with powerful tools for examining the structure and dynamics of membrane peptides and proteins. Here we briefly review the use of site-specific tryptophan fluorescence spectroscopy to probe aspects of peptide orientation, structure, and dynamics in lipid bilayers, focusing on recent developments in the literature.

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Language(s): eng - English
 Dates: 2002-03
 Publication Status: Published in print
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 Rev. Method: Peer
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Title: European Biophysics Journal
Source Genre: Journal
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Pages: - Volume / Issue: 31 (1) Sequence Number: - Start / End Page: 9 - 13 Identifier: -