English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

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

MPS-Authors
/persons/resource/persons14950

Clayton,  A. H. A.
Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society;

External Resource
No external resources are shared
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

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.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0012-F424-5
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.