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

来源：

CHEMICAL COMMUNICATIONS | 2012年 / 48卷 / 10期

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

页码：1550 / 1552

页数：3

共 32 条

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