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

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.

DOI: 10.1007/s002490100182

Cite this paper

@article{Clayton2002SitespecificTF, title={Site-specific tryptophan fluorescence spectroscopy as a probe of membrane peptide structure and dynamics}, author={Andrew H. A. Clayton and William H. Sawyer}, journal={European Biophysics Journal}, year={2002}, volume={31}, pages={9-13} }