Site-specific tryptophan fluorescence spectroscopy as a probe of membrane peptide structure and dynamics.
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.
Clayton
Andrew H A
AH
The Russell Grimwade School of Biochemistry and Molecular Biology, University of Melbourne, Parkville, Victoria, Australia. aclayto@gwdg.de
Sawyer
William H
WH
D055592:Biophysical Phenomena; D001703:Biophysics; D005454:Fluorescence Polarization; D008565:Membrane Proteins / Q000737:chemistry*; D015394:Molecular Structure; D011487:Protein Conformation; D013050:Spectrometry, Fluorescence; D013816:Thermodynamics; D014364:Tryptophan / Q000737:chemistry*
D008565:Membrane Proteins; D014364:Tryptophan