Site-specific tryptophan fluorescence spectroscopy as a probe of membrane peptide structure and dynamics
Site-specific tryptophan fluorescence spectroscopy as a probe of membrane peptide structure and dynamics
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DOI：
10.1007/s002490100182
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发表时间：
2002-03-01
影响因子：
2
通讯作者：
Sawyer, WH
中科院分区：
文献类型：
--
作者：
Clayton, AHA;Sawyer, WH
色氨酸的荧光包含有关吲哚侧链局部环境的有价值的信息。这种对环境的敏感性，再加上在多肽序列的特定位置合成或遗传结合单个色氨酸残基的能力，为膜生物物理学家提供了研究膜多肽和蛋白质的结构和动力学的强大工具。在这里，我们简要回顾了利用位点特异性色氨酸荧光光谱学来探测脂双层中肽的取向、结构和动力学的方面，重点介绍了文献中的最新进展。
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.