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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Revised version: 7 August 2001
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Clayton, A.H., Sawyer, W.H. Site-specific tryptophan fluorescence spectroscopy as a probe of membrane peptide structure and dynamics. Eur Biophys J 31, 9–13 (2002). https://doi.org/10.1007/s002490100182
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DOI: https://doi.org/10.1007/s002490100182