Thioamide quenching of intrinsic protein fluorescence

被引:58
作者
Goldberg, Jacob M. [1 ]
Wissner, Rebecca F. [1 ]
Klein, Alyssa M. [1 ]
Petersson, E. James [1 ]
机构
[1] Univ Penn, Dept Chem, Philadelphia, PA 19104 USA
基金
美国国家科学基金会;
关键词
RESONANCE ENERGY-TRANSFER; TRYPTOPHAN FLUORESCENCE; BINDING; CALMODULIN; ELECTRON; CALCIUM; TYROSINE; PEPTIDE; PROBES;
D O I
10.1039/c1cc14708k
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Thioamides quench tryptophan and tyrosine fluorescence in a distance-dependent manner and thus can be used to monitor the binding of thioamide-containing peptides to proteins. Since thioamide analogs of the natural amino acids can be synthetically incorporated into peptides, they can function as minimally-perturbing probes of protein/peptide interactions.
引用
收藏
页码:1550 / 1552
页数:3
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