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

被引：0

作者：

Andrew H. Clayton

William H. Sawyer

机构：

[1] The Russell Grimwade School of Biochemistry and Molecular Biology,

[2] University of Melbourne,undefined

[3] Parkville,undefined

[4] Victoria 3052,undefined

[5] Australia,undefined

[6] Present address: Department of Molecular Biology,undefined

[7] Max Planck Institute for Biophysical Chemistry,undefined

[8] 37077 Göttingen,undefined

[9] Germany,undefined

[10] E-mail: aclayto@gwdg.de,undefined

[11] Fax: +49-551-2011467,undefined

来源：

European Biophysics Journal | 2002年 / 31卷

关键词：

Tryptophan Dynamics Amphipathic helix Lipid-protein interactions Time-resolved fluorescence spectroscopy;

D O I：

暂无

中图分类号：

学科分类号：

摘要：

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.

引用

页码：9 / 13

页数：4

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