On the use of thioamides as fluorescence quenching probes for tracking protein folding and stability

被引：47

作者：

Petersson, E. James ^{[1
]}

Goldberg, Jacob M. ^{[1
]}

Wissner, Rebecca F. ^{[1
]}

机构：

[1] Univ Penn, Dept Chem, Philadelphia, PA 19104 USA

来源：

PHYSICAL CHEMISTRY CHEMICAL PHYSICS | 2014年 / 16卷 / 15期

基金：

美国国家科学基金会;

关键词：

PHOTOINDUCED ELECTRON-TRANSFER; COENZYME-M REDUCTASE; ENERGY-TRANSFER; TARGET RECOGNITION; CRYSTAL-STRUCTURE; SINGLE-MOLECULE; DYNAMICS; PEPTIDES; SPECTRA; SPECTROSCOPY;

D O I：

10.1039/c3cp55525a

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

Our laboratory has developed thioamide analogs of the natural amino acids as minimally-perturbing fluorescence quenching probes that can be placed at many locations in a protein sequence. We have shown that the mechanism of quenching can be either Forster resonance energy transfer (FRET) or photoinduced electron transfer (PET), depending on the identity of the donor fluorophore. Furthermore, we have shown that one can use a combination of semi-synthetic methods to label full-sized proteins with fluorophore-thioamide pairs. These probes can be used to study protein-protein interactions, protein folding or misfolding, and proteolysis.

引用

页码：6827 / 6837

页数：11

共 69 条

[31] ULTRAVIOLET ABSORPTION SPECTRA OF AQUEOUS SOLUTIONS AND SINGLE CRYSTALS OF THIOACETAMIDE AND THIOUREA [J].