Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 135, Issue 49, Pages 18651-18658Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja409709x
Keywords
-
Categories
Funding
- University of Pennsylvania
- Alfred P. Sloan Foundation [BR2012-085]
- National Science Foundation [NSF CHE-1150351]
- National Institutes of Health [NIH NS081033]
- NIH [RR-023444, P41GM104605]
- NSF [MRI-0820996]
- Parkinson's Disease Foundation
- Penn Undergraduate Research Mentorship program
- Direct For Mathematical & Physical Scien
- Division Of Chemistry [1150351] Funding Source: National Science Foundation
Ask authors/readers for more resources
Previously we have shown that thioamides can be incorporated into proteins as minimally perturbing fluorescence-quenching probes to study protein dynamics, folding, and aggregation. Here, we show that the spontaneity of photoinduced electron transfer between a thioamide and an excited fluorophore is governed by the redox potentials of each moiety according to a Rehm-Weller-type model, We have used this model to predict thioamide quenching of various common fluorophores, and we rigorously tested more than a dozen examples. In each case, we found excellent agreement between our theoretical predictions and experimental observations. In this way, we have been able to expand the scope of fluorophores quenched by thioamides to include dyes suitable for microscopy and single-molecule studies, including fluorescein, Alexa Fluor 488, BODIPY FL, and rhodamine 6G. We describe the photochemistry of these systems and explore applications that demonstrate the utility of thioamide quenching of fluorescein to studying protein folding and proteolysis.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available