Site-specific tryptophan fluorescence spectroscopy as a probe of membrane peptide structure and dynamics.
Andrew HA Clayton, William H Sawyer
European Biophysics Journal with Biophysics Letters | Springer Science and Business Media LLC | Published : 2002
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.