Jump to main content
Jump to site search

Issue 15, 2014
Previous Article Next Article

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

Author affiliations

Abstract

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 Förster 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.

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

Back to tab navigation

Publication details

The article was received on 31 Dec 2013, accepted on 27 Feb 2014 and first published on 06 Mar 2014


Article type: Perspective
DOI: 10.1039/C3CP55525A
Author version
available:
Download author version (PDF)
Phys. Chem. Chem. Phys., 2014,16, 6827-6837

  •   Request permissions

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

    E. J. Petersson, J. M. Goldberg and R. F. Wissner, Phys. Chem. Chem. Phys., 2014, 16, 6827
    DOI: 10.1039/C3CP55525A

Search articles by author

Spotlight

Advertisements